TY  - JOUR
AU  - Degrassi, Giuliano
AU  - Mortato, Valentina
AU  - Devescovi, Giulia
AU  - Hoshino, Rodrigo
AU  - Chatnaparat, Tiyakhon
AU  - Kojić, Milan
AU  - Carpentieri-Pipolo, Valeria
AU  - Zhao, Youfu
AU  - Venturi, Vittorio
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1232
AB  - Many plant bacterial pathogens monitor their group behaviour and their population density via production of N-acyl homoserine lactone signals which regulate the expression of several genes via the LuxI/R homologs. This regulatory network, termed quorum sensing (QS), is present in the soybean bacterial pathogen Pseudomonas savastanoi pv glycinea (Psg). The sequenced genomes of two strains of Psg, race 4 and B076, contain an N-acyl homoserine lactone (AHL) based LuxI/R QS system named AhlI/R. While studying the QS system of Psg strains race 4 and B076 isolated in USA, LMG5066 in New Zealand and IBSBF355 in Brazil, we found that B076, LMG5066 and IBSBF355 possess a point mutation in the ahlR gene that causes a frameshift resulting in a truncated AhlR protein. Psg race 4 does not possess the mutation in ahlR and the QS system is functional. The same mutation in the ahlR genewas found to be also present in 9 of 19 Psg strains isolated from diseased soybean in Illinois. Phenotypic analysis of strains showed that swarming motility is repressed whereas phosphate solubilisation was activated by QS in Psg. Analysing the secretome, we also found that four proteins were under QS regulation.
PB  - Oxford Univ Press, Oxford
T2  - FEMS Microbiology Letters
T1  - Many plant pathogenic Pseudomonas savastanoi pv glycinea isolates possess an inactive quorum sensing ahlR gene via a point mutation
IS  - 12
VL  - 366
DO  - 10.1093/femsle/fnz149
ER  - 

@article{
author = "Degrassi, Giuliano and Mortato, Valentina and Devescovi, Giulia and Hoshino, Rodrigo and Chatnaparat, Tiyakhon and Kojić, Milan and Carpentieri-Pipolo, Valeria and Zhao, Youfu and Venturi, Vittorio",
year = "2019",
abstract = "Many plant bacterial pathogens monitor their group behaviour and their population density via production of N-acyl homoserine lactone signals which regulate the expression of several genes via the LuxI/R homologs. This regulatory network, termed quorum sensing (QS), is present in the soybean bacterial pathogen Pseudomonas savastanoi pv glycinea (Psg). The sequenced genomes of two strains of Psg, race 4 and B076, contain an N-acyl homoserine lactone (AHL) based LuxI/R QS system named AhlI/R. While studying the QS system of Psg strains race 4 and B076 isolated in USA, LMG5066 in New Zealand and IBSBF355 in Brazil, we found that B076, LMG5066 and IBSBF355 possess a point mutation in the ahlR gene that causes a frameshift resulting in a truncated AhlR protein. Psg race 4 does not possess the mutation in ahlR and the QS system is functional. The same mutation in the ahlR genewas found to be also present in 9 of 19 Psg strains isolated from diseased soybean in Illinois. Phenotypic analysis of strains showed that swarming motility is repressed whereas phosphate solubilisation was activated by QS in Psg. Analysing the secretome, we also found that four proteins were under QS regulation.",
publisher = "Oxford Univ Press, Oxford",
journal = "FEMS Microbiology Letters",
title = "Many plant pathogenic Pseudomonas savastanoi pv glycinea isolates possess an inactive quorum sensing ahlR gene via a point mutation",
number = "12",
volume = "366",
doi = "10.1093/femsle/fnz149"
}

Degrassi, G., Mortato, V., Devescovi, G., Hoshino, R., Chatnaparat, T., Kojić, M., Carpentieri-Pipolo, V., Zhao, Y.,& Venturi, V.. (2019). Many plant pathogenic Pseudomonas savastanoi pv glycinea isolates possess an inactive quorum sensing ahlR gene via a point mutation. in FEMS Microbiology Letters
Oxford Univ Press, Oxford., 366(12).
https://doi.org/10.1093/femsle/fnz149

Degrassi G, Mortato V, Devescovi G, Hoshino R, Chatnaparat T, Kojić M, Carpentieri-Pipolo V, Zhao Y, Venturi V. Many plant pathogenic Pseudomonas savastanoi pv glycinea isolates possess an inactive quorum sensing ahlR gene via a point mutation. in FEMS Microbiology Letters. 2019;366(12).
doi:10.1093/femsle/fnz149 .

Degrassi, Giuliano, Mortato, Valentina, Devescovi, Giulia, Hoshino, Rodrigo, Chatnaparat, Tiyakhon, Kojić, Milan, Carpentieri-Pipolo, Valeria, Zhao, Youfu, Venturi, Vittorio, "Many plant pathogenic Pseudomonas savastanoi pv glycinea isolates possess an inactive quorum sensing ahlR gene via a point mutation" in FEMS Microbiology Letters, 366, no. 12 (2019),
https://doi.org/10.1093/femsle/fnz149 . .

TY  - JOUR
AU  - Devescovi, Giulia
AU  - Kojić, Milan
AU  - Covaceuszach, Sonia
AU  - Cymara, Miguel
AU  - Williams, Paul
AU  - Bertani, Iris
AU  - Subramoni, Sujatha
AU  - Venturi, Vittorio
PY  - 2017
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1052
AB  - In Chromobacteium violaceum, the purple pigment violacein is under positive regulation by the N-acylhomoserine lactone CviI/R quorum sensing system and negative regulation by an uncharacterized putative repressor. In this study we report that the biosynthesis of violacein is negatively controlled by a novel repressor protein, VioS. The violacein operon is regulated negatively by VioS and positively by the CviI/R system in both C. violaceum and in a heterologous Escherichia coli genetic background. VioS does not regulate the CviI/R system and apart from violacein, VioS, and quorum sensing regulate other phenotypes antagonistically. Quorum sensing regulated phenotypes in C. violaceum are therefore further regulated providing an additional level of control.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Negative Regulation of Violacein Biosynthesis in Chromobacterium violaceum
VL  - 8
DO  - 10.3389/fmicb.2017.00349
ER  - 

@article{
author = "Devescovi, Giulia and Kojić, Milan and Covaceuszach, Sonia and Cymara, Miguel and Williams, Paul and Bertani, Iris and Subramoni, Sujatha and Venturi, Vittorio",
year = "2017",
abstract = "In Chromobacteium violaceum, the purple pigment violacein is under positive regulation by the N-acylhomoserine lactone CviI/R quorum sensing system and negative regulation by an uncharacterized putative repressor. In this study we report that the biosynthesis of violacein is negatively controlled by a novel repressor protein, VioS. The violacein operon is regulated negatively by VioS and positively by the CviI/R system in both C. violaceum and in a heterologous Escherichia coli genetic background. VioS does not regulate the CviI/R system and apart from violacein, VioS, and quorum sensing regulate other phenotypes antagonistically. Quorum sensing regulated phenotypes in C. violaceum are therefore further regulated providing an additional level of control.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Negative Regulation of Violacein Biosynthesis in Chromobacterium violaceum",
volume = "8",
doi = "10.3389/fmicb.2017.00349"
}

Devescovi, G., Kojić, M., Covaceuszach, S., Cymara, M., Williams, P., Bertani, I., Subramoni, S.,& Venturi, V.. (2017). Negative Regulation of Violacein Biosynthesis in Chromobacterium violaceum. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 8.
https://doi.org/10.3389/fmicb.2017.00349

Devescovi G, Kojić M, Covaceuszach S, Cymara M, Williams P, Bertani I, Subramoni S, Venturi V. Negative Regulation of Violacein Biosynthesis in Chromobacterium violaceum. in Frontiers in Microbiology. 2017;8.
doi:10.3389/fmicb.2017.00349 .

Devescovi, Giulia, Kojić, Milan, Covaceuszach, Sonia, Cymara, Miguel, Williams, Paul, Bertani, Iris, Subramoni, Sujatha, Venturi, Vittorio, "Negative Regulation of Violacein Biosynthesis in Chromobacterium violaceum" in Frontiers in Microbiology, 8 (2017),
https://doi.org/10.3389/fmicb.2017.00349 . .

TY  - JOUR
AU  - Miljković, Marija
AU  - Bertani, Iris
AU  - Fira, Đorđe
AU  - Jovčić, Branko
AU  - Novović, Katarina
AU  - Venturi, Vittorio
AU  - Kojić, Milan
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/924
AB  - AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation
EP  - 14
SP  - 1
VL  - 7
DO  - 10.3389/fmicb.2016.01422
ER  - 

@article{
author = "Miljković, Marija and Bertani, Iris and Fira, Đorđe and Jovčić, Branko and Novović, Katarina and Venturi, Vittorio and Kojić, Milan",
year = "2016",
abstract = "AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation",
pages = "14-1",
volume = "7",
doi = "10.3389/fmicb.2016.01422"
}

Miljković, M., Bertani, I., Fira, Đ., Jovčić, B., Novović, K., Venturi, V.,& Kojić, M.. (2016). Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 7, 1-14.
https://doi.org/10.3389/fmicb.2016.01422

Miljković M, Bertani I, Fira Đ, Jovčić B, Novović K, Venturi V, Kojić M. Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation. in Frontiers in Microbiology. 2016;7:1-14.
doi:10.3389/fmicb.2016.01422 .

Miljković, Marija, Bertani, Iris, Fira, Đorđe, Jovčić, Branko, Novović, Katarina, Venturi, Vittorio, Kojić, Milan, "Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation" in Frontiers in Microbiology, 7 (2016):1-14,
https://doi.org/10.3389/fmicb.2016.01422 . .

TY  - JOUR
AU  - Miljković, Marija
AU  - Uzelac, Gordana
AU  - Mirković, Nemanja
AU  - Devescovi, Giulia
AU  - Diep, Dzung B.
AU  - Venturi, Vittorio
AU  - Kojić, Milan
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/904
AB  - The Zn-dependent membrane-located protease YvjB has previously been shown to serve as a target receptor for LsbB, a class II leaderless lactococcal bacteriocin. Although yvjB is highly conserved in the genus Lactococcus, the bacteriocin appears to be active only against the subspecies L. lactis subsp. lactis. Comparative analysis of the YvjB proteins of a sensitive strain (YvjB(MN)) and a resistant strain (YvjB(MG)) showed that they differ from each other in 31 positions. In this study, we applied site-directed mutagenesis and performed directed binding studies to provide biochemical evidence that LsbB interacts with the third transmembrane helix of YvjB in susceptible cells. The site-directed mutagenesis of LsbB and YvjB proteins showed that certain amino acids and the length of LsbB are responsible for the bacteriocin activity, most probably through adequate interaction of these two proteins; the essential amino acids in LsbB responsible for the activity are tryptophan (Trp(25)) and terminal alanine (Ala(30)). It was also shown that the distance between Trp(25) and terminal alanine is crucial for LsbB activity. The crucial region in YvjB for the interaction with LsbB is the beginning of the third transmembrane helix, particularly amino acids tyrosine (Tyr(356)) and alanine (Ala(353)). In vitro experiments showed that LsbB could interact with both YvjB(MN) and YvjB(MG), but the strength of interaction is significantly less with YvjB(MG). In vivo experiments with immunofluorescently labeled antibody demonstrated that LsbB specifically interacts only with cells carrying YvjB(MN). IMPORTANCE The antimicrobial activity of LsbB bacteriocin depends on the correct interaction with the corresponding receptor in the bacterial membrane of sensitive cells. Membrane-located bacteriocin receptors have essential primary functions, such as cell wall synthesis or sugar transport, and it seems that interaction with bacteriocins is suicidal for cells. This study showed that the C-terminal part of LsbB is crucial for the bacteriocin activity, most probably through adequate interaction with the third transmembrane domain of the YvjB receptor. The conserved Tyr(356) and Ala(353) residues of YvjB are essential for the function of this Zn-dependent membrane-located protease as a bacteriocin receptor.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor
EP  - 5374
IS  - 17
SP  - 5364
VL  - 82
DO  - 10.1128/AEM.01293-16
ER  - 

@article{
author = "Miljković, Marija and Uzelac, Gordana and Mirković, Nemanja and Devescovi, Giulia and Diep, Dzung B. and Venturi, Vittorio and Kojić, Milan",
year = "2016",
abstract = "The Zn-dependent membrane-located protease YvjB has previously been shown to serve as a target receptor for LsbB, a class II leaderless lactococcal bacteriocin. Although yvjB is highly conserved in the genus Lactococcus, the bacteriocin appears to be active only against the subspecies L. lactis subsp. lactis. Comparative analysis of the YvjB proteins of a sensitive strain (YvjB(MN)) and a resistant strain (YvjB(MG)) showed that they differ from each other in 31 positions. In this study, we applied site-directed mutagenesis and performed directed binding studies to provide biochemical evidence that LsbB interacts with the third transmembrane helix of YvjB in susceptible cells. The site-directed mutagenesis of LsbB and YvjB proteins showed that certain amino acids and the length of LsbB are responsible for the bacteriocin activity, most probably through adequate interaction of these two proteins; the essential amino acids in LsbB responsible for the activity are tryptophan (Trp(25)) and terminal alanine (Ala(30)). It was also shown that the distance between Trp(25) and terminal alanine is crucial for LsbB activity. The crucial region in YvjB for the interaction with LsbB is the beginning of the third transmembrane helix, particularly amino acids tyrosine (Tyr(356)) and alanine (Ala(353)). In vitro experiments showed that LsbB could interact with both YvjB(MN) and YvjB(MG), but the strength of interaction is significantly less with YvjB(MG). In vivo experiments with immunofluorescently labeled antibody demonstrated that LsbB specifically interacts only with cells carrying YvjB(MN). IMPORTANCE The antimicrobial activity of LsbB bacteriocin depends on the correct interaction with the corresponding receptor in the bacterial membrane of sensitive cells. Membrane-located bacteriocin receptors have essential primary functions, such as cell wall synthesis or sugar transport, and it seems that interaction with bacteriocins is suicidal for cells. This study showed that the C-terminal part of LsbB is crucial for the bacteriocin activity, most probably through adequate interaction with the third transmembrane domain of the YvjB receptor. The conserved Tyr(356) and Ala(353) residues of YvjB are essential for the function of this Zn-dependent membrane-located protease as a bacteriocin receptor.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor",
pages = "5374-5364",
number = "17",
volume = "82",
doi = "10.1128/AEM.01293-16"
}

Miljković, M., Uzelac, G., Mirković, N., Devescovi, G., Diep, D. B., Venturi, V.,& Kojić, M.. (2016). LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 82(17), 5364-5374.
https://doi.org/10.1128/AEM.01293-16

Miljković M, Uzelac G, Mirković N, Devescovi G, Diep DB, Venturi V, Kojić M. LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor. in Applied and Environmental Microbiology. 2016;82(17):5364-5374.
doi:10.1128/AEM.01293-16 .

Miljković, Marija, Uzelac, Gordana, Mirković, Nemanja, Devescovi, Giulia, Diep, Dzung B., Venturi, Vittorio, Kojić, Milan, "LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor" in Applied and Environmental Microbiology, 82, no. 17 (2016):5364-5374,
https://doi.org/10.1128/AEM.01293-16 . .

TY  - JOUR
AU  - Berić, Tanja
AU  - Kojić, Milan
AU  - Stanković, Slaviša
AU  - Topisirović, Ljubiša
AU  - Degrassi, Giuliano
AU  - Myers, Michael
AU  - Venturi, Vittorio
AU  - Fira, Đorđe
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/574
AB  - Screening of 203 Bacillus sp. natural isolates for antimicrobial activity against phytopathogenic bacteria showed that 127 tested strains inhibit at least one sensitive strain, which illustrates their potential use as biocontrol agents. Among them, 104 isolates showed significant antagonism against Xanthomonas oryzae pv. oryzae, and only one of these (VPS50.2) synthesizes bacteriocin. An additional screening tested whether 51 isolates contained genes involved in the biosynthesis of lipopeptides of the iturin and surfactin classes. Results show that 33 isolates harbour the operon for iturin biosynthesis, and six of them carry the sfp gene, responsible for the biosynthesis of surfactin. Lipopeptide purification from the supernatant of isolate SS12.9 (identified as B. subtilis or B. amyloliquefaciens) was performed using ethyl acetate extraction, ultrafiltration and reversed phase HPLC. Mass spectrometry analysis confirmed that isolate SS12.9 produces a substance of the iturin class with potential for biocontrol of X. oryzae pv. oryzae.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria
EP  - 31
IS  - 1
SP  - 25
VL  - 50
UR  - https://hdl.handle.net/21.15107/rcub_imagine_574
ER  - 

@article{
author = "Berić, Tanja and Kojić, Milan and Stanković, Slaviša and Topisirović, Ljubiša and Degrassi, Giuliano and Myers, Michael and Venturi, Vittorio and Fira, Đorđe",
year = "2012",
abstract = "Screening of 203 Bacillus sp. natural isolates for antimicrobial activity against phytopathogenic bacteria showed that 127 tested strains inhibit at least one sensitive strain, which illustrates their potential use as biocontrol agents. Among them, 104 isolates showed significant antagonism against Xanthomonas oryzae pv. oryzae, and only one of these (VPS50.2) synthesizes bacteriocin. An additional screening tested whether 51 isolates contained genes involved in the biosynthesis of lipopeptides of the iturin and surfactin classes. Results show that 33 isolates harbour the operon for iturin biosynthesis, and six of them carry the sfp gene, responsible for the biosynthesis of surfactin. Lipopeptide purification from the supernatant of isolate SS12.9 (identified as B. subtilis or B. amyloliquefaciens) was performed using ethyl acetate extraction, ultrafiltration and reversed phase HPLC. Mass spectrometry analysis confirmed that isolate SS12.9 produces a substance of the iturin class with potential for biocontrol of X. oryzae pv. oryzae.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria",
pages = "31-25",
number = "1",
volume = "50",
url = "https://hdl.handle.net/21.15107/rcub_imagine_574"
}

Berić, T., Kojić, M., Stanković, S., Topisirović, L., Degrassi, G., Myers, M., Venturi, V.,& Fira, Đ.. (2012). Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria. in Food Technology and Biotechnology
University of Zagreb., 50(1), 25-31.
https://hdl.handle.net/21.15107/rcub_imagine_574

Berić T, Kojić M, Stanković S, Topisirović L, Degrassi G, Myers M, Venturi V, Fira Đ. Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria. in Food Technology and Biotechnology. 2012;50(1):25-31.
https://hdl.handle.net/21.15107/rcub_imagine_574 .

Berić, Tanja, Kojić, Milan, Stanković, Slaviša, Topisirović, Ljubiša, Degrassi, Giuliano, Myers, Michael, Venturi, Vittorio, Fira, Đorđe, "Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria" in Food Technology and Biotechnology, 50, no. 1 (2012):25-31,
https://hdl.handle.net/21.15107/rcub_imagine_574 .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Venturi, Vittorio
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/534
AB  - Pseudomonas sp. strain ATCC19151 is a natural isolate from sewage with the ability to degrade detergents. Genes encoding potential choline sulfatase (betC), substrate-binding ABC transporter protein (betD), sulfate transporter (betE), and divergent putative transcriptional regulator (betR) were cloned and characterized from strain ATCC19151. In silico analysis revealed that (1) the BetC protein belongs to alkPPc superfamily and shares CXPXR sequence with the cysteine sulfatases of group I, (2) BetR belongs to the LysR family of transcriptional regulators, (3) BetD is part of the PBPb superfamily of periplasmic and membrane-associated proteins, and (4) BetE is a permease and contains STAS domain. Insertional mutagenesis and genetic complementation show that betC gene encodes a functional choline sulfatase. Analysis of the betC (P (betC) ) and betR (P (betR) ) promoters revealed that they are inducible. BetR activates betC and betR transcription in the presence of choline sulfate, whilst in the absence of choline sulfate, BetR represses its own transcription. It was further established that BetR directly binds to betC-betR intergenic region in vitro, with higher affinity in the presence of choline sulfate as cofactor. Transcription of betC and betR was not induced in the presence of high concentration of NaCl.
PB  - Springer, New York
T2  - Archives of Microbiology
T1  - Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151
EP  - 405
IS  - 6
SP  - 399
VL  - 193
DO  - 10.1007/s00203-011-0685-x
ER  - 

@article{
author = "Jovčić, Branko and Venturi, Vittorio and Topisirović, Ljubiša and Kojić, Milan",
year = "2011",
abstract = "Pseudomonas sp. strain ATCC19151 is a natural isolate from sewage with the ability to degrade detergents. Genes encoding potential choline sulfatase (betC), substrate-binding ABC transporter protein (betD), sulfate transporter (betE), and divergent putative transcriptional regulator (betR) were cloned and characterized from strain ATCC19151. In silico analysis revealed that (1) the BetC protein belongs to alkPPc superfamily and shares CXPXR sequence with the cysteine sulfatases of group I, (2) BetR belongs to the LysR family of transcriptional regulators, (3) BetD is part of the PBPb superfamily of periplasmic and membrane-associated proteins, and (4) BetE is a permease and contains STAS domain. Insertional mutagenesis and genetic complementation show that betC gene encodes a functional choline sulfatase. Analysis of the betC (P (betC) ) and betR (P (betR) ) promoters revealed that they are inducible. BetR activates betC and betR transcription in the presence of choline sulfate, whilst in the absence of choline sulfate, BetR represses its own transcription. It was further established that BetR directly binds to betC-betR intergenic region in vitro, with higher affinity in the presence of choline sulfate as cofactor. Transcription of betC and betR was not induced in the presence of high concentration of NaCl.",
publisher = "Springer, New York",
journal = "Archives of Microbiology",
title = "Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151",
pages = "405-399",
number = "6",
volume = "193",
doi = "10.1007/s00203-011-0685-x"
}

Jovčić, B., Venturi, V., Topisirović, L.,& Kojić, M.. (2011). Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151. in Archives of Microbiology
Springer, New York., 193(6), 399-405.
https://doi.org/10.1007/s00203-011-0685-x

Jovčić B, Venturi V, Topisirović L, Kojić M. Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151. in Archives of Microbiology. 2011;193(6):399-405.
doi:10.1007/s00203-011-0685-x .

Jovčić, Branko, Venturi, Vittorio, Topisirović, Ljubiša, Kojić, Milan, "Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151" in Archives of Microbiology, 193, no. 6 (2011):399-405,
https://doi.org/10.1007/s00203-011-0685-x . .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Venturi, V.
AU  - Davison, J.
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/452
AB  - Aims: The presented study was aimed to reveal transcriptional regulation of genes involved in SDS degradation (sdsA and sdsB) in Pseudomonas sp. ATCC19151. In addition, the ability of Pseudomonas sp. ATCC19151 to degrade anionic surfactants present in commercial detergent and septic tank drain was analysed. Methods and Results: Strain ATCC19151, at 30 degrees C, degrades all SDS present in the liquid medium (up to 4% w/v of SDS) within 48 h. ATCC19151 grows in the presence up to 15% (v/v) 'Fairy' commercial detergent and mineralizes 35% of present anionic surfactants. Analysis of the sdsA (P(sdsA)) and divergent sdsB (P(sdsB)) gene promoter activities revealed that SdsB acts as a positive regulator of sdsA and sdsB transcription. P(sdsA) and P(sdsB) activities rose significantly in the presence of the SDS, indicating inducibility of sdsA and sdsB transcription. DNA-binding assay indicated that SdsB directly regulates the transcription of sdsA and sdsB genes. Strain ATCC19151 grew in a sterile septic tank drain and on commercial detergent as sole source of carbon. Conclusions: SdsA enables Pseudomonas sp. ATCC19151 to utilize SDS as a sole carbon source. SdsB is positive transcriptional regulator of sdsA and sdsB genes. Significance and Impact of the Study: Ability of ATCC19151 to degrade anionic surfactants makes Pseudomonas sp. ATCC19151 a good candidate for bioremediation.
PB  - Wiley-Blackwell, Malden
T2  - Journal of Applied Microbiology
T1  - Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants
EP  - 1083
IS  - 3
SP  - 1076
VL  - 109
DO  - 10.1111/j.1365-2672.2010.04738.x
ER  - 

@article{
author = "Jovčić, Branko and Venturi, V. and Davison, J. and Topisirović, Ljubiša and Kojić, Milan",
year = "2010",
abstract = "Aims: The presented study was aimed to reveal transcriptional regulation of genes involved in SDS degradation (sdsA and sdsB) in Pseudomonas sp. ATCC19151. In addition, the ability of Pseudomonas sp. ATCC19151 to degrade anionic surfactants present in commercial detergent and septic tank drain was analysed. Methods and Results: Strain ATCC19151, at 30 degrees C, degrades all SDS present in the liquid medium (up to 4% w/v of SDS) within 48 h. ATCC19151 grows in the presence up to 15% (v/v) 'Fairy' commercial detergent and mineralizes 35% of present anionic surfactants. Analysis of the sdsA (P(sdsA)) and divergent sdsB (P(sdsB)) gene promoter activities revealed that SdsB acts as a positive regulator of sdsA and sdsB transcription. P(sdsA) and P(sdsB) activities rose significantly in the presence of the SDS, indicating inducibility of sdsA and sdsB transcription. DNA-binding assay indicated that SdsB directly regulates the transcription of sdsA and sdsB genes. Strain ATCC19151 grew in a sterile septic tank drain and on commercial detergent as sole source of carbon. Conclusions: SdsA enables Pseudomonas sp. ATCC19151 to utilize SDS as a sole carbon source. SdsB is positive transcriptional regulator of sdsA and sdsB genes. Significance and Impact of the Study: Ability of ATCC19151 to degrade anionic surfactants makes Pseudomonas sp. ATCC19151 a good candidate for bioremediation.",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of Applied Microbiology",
title = "Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants",
pages = "1083-1076",
number = "3",
volume = "109",
doi = "10.1111/j.1365-2672.2010.04738.x"
}

Jovčić, B., Venturi, V., Davison, J., Topisirović, L.,& Kojić, M.. (2010). Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants. in Journal of Applied Microbiology
Wiley-Blackwell, Malden., 109(3), 1076-1083.
https://doi.org/10.1111/j.1365-2672.2010.04738.x

Jovčić B, Venturi V, Davison J, Topisirović L, Kojić M. Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants. in Journal of Applied Microbiology. 2010;109(3):1076-1083.
doi:10.1111/j.1365-2672.2010.04738.x .

Jovčić, Branko, Venturi, V., Davison, J., Topisirović, Ljubiša, Kojić, Milan, "Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants" in Journal of Applied Microbiology, 109, no. 3 (2010):1076-1083,
https://doi.org/10.1111/j.1365-2672.2010.04738.x . .

TY  - JOUR
AU  - Jovčić, Branko
AU  - Bertani, Iris
AU  - Venturi, Vittorio
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2008
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/333
AB  - The sigma(S) subunit of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genes in Gram-negative bacteria. The Pseudomonas putida rpoS gene is transcribed as a monocistronic rpoS mRNA with a 368 nucleotide-long 5' untranslated region (5' UTR). In this study, we investigate the posttranscriptional control of RpoS synthesis using rpoS-lacZ transcriptional and translational fusions consisting of the native promoter and deletions of 5' UTR or insertion into UTR. The differing activity of constructed translational fusions strongly indicated that the 5' UTR is involved in the translational regulation of RpoS expression in the stationary phase. The results obtained herein demonstrated that the structure of UTR performs an important function in the translational regulation of the rpoS gene.
PB  - Microbiology Soc Korea, Seoul
T2  - Journal of Microbiology
T1  - 5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation
EP  - 61
IS  - 1
SP  - 56
VL  - 46
DO  - 10.1007/s12275-007-0127-2
ER  - 

@article{
author = "Jovčić, Branko and Bertani, Iris and Venturi, Vittorio and Topisirović, Ljubiša and Kojić, Milan",
year = "2008",
abstract = "The sigma(S) subunit of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genes in Gram-negative bacteria. The Pseudomonas putida rpoS gene is transcribed as a monocistronic rpoS mRNA with a 368 nucleotide-long 5' untranslated region (5' UTR). In this study, we investigate the posttranscriptional control of RpoS synthesis using rpoS-lacZ transcriptional and translational fusions consisting of the native promoter and deletions of 5' UTR or insertion into UTR. The differing activity of constructed translational fusions strongly indicated that the 5' UTR is involved in the translational regulation of RpoS expression in the stationary phase. The results obtained herein demonstrated that the structure of UTR performs an important function in the translational regulation of the rpoS gene.",
publisher = "Microbiology Soc Korea, Seoul",
journal = "Journal of Microbiology",
title = "5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation",
pages = "61-56",
number = "1",
volume = "46",
doi = "10.1007/s12275-007-0127-2"
}

Jovčić, B., Bertani, I., Venturi, V., Topisirović, L.,& Kojić, M.. (2008). 5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation. in Journal of Microbiology
Microbiology Soc Korea, Seoul., 46(1), 56-61.
https://doi.org/10.1007/s12275-007-0127-2

Jovčić B, Bertani I, Venturi V, Topisirović L, Kojić M. 5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation. in Journal of Microbiology. 2008;46(1):56-61.
doi:10.1007/s12275-007-0127-2 .

Jovčić, Branko, Bertani, Iris, Venturi, Vittorio, Topisirović, Ljubiša, Kojić, Milan, "5 ' untranslated region of the Pseudomonas putida WCS358 stationary phase sigma factor rpoS mRNA is involved in RpoS translational regulation" in Journal of Microbiology, 46, no. 1 (2008):56-61,
https://doi.org/10.1007/s12275-007-0127-2 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Jovčić, Branko
AU  - Vindigni, A
AU  - Odreman, F
AU  - Venturi, V
PY  - 2005
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/225
AB  - The PsrA transcriptional regulator is involved in stationary phase induced transcriptional regulation of rpoS and in negative auto-regulation in Pseudomonas aeruginosa. This study was designed to determine whether other loci were regulated by PsrA in P. aeruginosa. Computer search was performed of the PsrA binding motif (G/CAAAC N2-4 GTTTG/C) against the P. aeruginosa genome sequence. Four of 14 analysed promoters responded to and bound PsrA; (i) divergent promoters controlling PA2952/ PA2951 and PA2953, (ii) promoter of PA0506 and (iii) upstream region of PA3571. Promoters PA0506 and PA2952-PA2951 were regulated negatively whereas promoters of PA2953 and PA3571 were regulated positively by PsrA. Two dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (21) SDS-PAGE) analysis on total proteins from P. aeruginosa PAO1 and psrA knock-out derivative was also performed resulting in the identification of 11 protein spots which were differentially regulated. These studies have indicated PsrA as a global regulator.
PB  - Wiley-Blackwell, Hoboken
T2  - FEMS Microbiology Letters
T1  - Novel target genes of PsrA transcriptional regulator of Pseudomonas aeruginosa
EP  - 181
IS  - 2
SP  - 175
VL  - 246
DO  - 10.1016/j.femsle.2005.04.003
ER  - 

@article{
author = "Kojić, Milan and Jovčić, Branko and Vindigni, A and Odreman, F and Venturi, V",
year = "2005",
abstract = "The PsrA transcriptional regulator is involved in stationary phase induced transcriptional regulation of rpoS and in negative auto-regulation in Pseudomonas aeruginosa. This study was designed to determine whether other loci were regulated by PsrA in P. aeruginosa. Computer search was performed of the PsrA binding motif (G/CAAAC N2-4 GTTTG/C) against the P. aeruginosa genome sequence. Four of 14 analysed promoters responded to and bound PsrA; (i) divergent promoters controlling PA2952/ PA2951 and PA2953, (ii) promoter of PA0506 and (iii) upstream region of PA3571. Promoters PA0506 and PA2952-PA2951 were regulated negatively whereas promoters of PA2953 and PA3571 were regulated positively by PsrA. Two dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (21) SDS-PAGE) analysis on total proteins from P. aeruginosa PAO1 and psrA knock-out derivative was also performed resulting in the identification of 11 protein spots which were differentially regulated. These studies have indicated PsrA as a global regulator.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEMS Microbiology Letters",
title = "Novel target genes of PsrA transcriptional regulator of Pseudomonas aeruginosa",
pages = "181-175",
number = "2",
volume = "246",
doi = "10.1016/j.femsle.2005.04.003"
}

Kojić, M., Jovčić, B., Vindigni, A., Odreman, F.,& Venturi, V.. (2005). Novel target genes of PsrA transcriptional regulator of Pseudomonas aeruginosa. in FEMS Microbiology Letters
Wiley-Blackwell, Hoboken., 246(2), 175-181.
https://doi.org/10.1016/j.femsle.2005.04.003

Kojić M, Jovčić B, Vindigni A, Odreman F, Venturi V. Novel target genes of PsrA transcriptional regulator of Pseudomonas aeruginosa. in FEMS Microbiology Letters. 2005;246(2):175-181.
doi:10.1016/j.femsle.2005.04.003 .

Kojić, Milan, Jovčić, Branko, Vindigni, A, Odreman, F, Venturi, V, "Novel target genes of PsrA transcriptional regulator of Pseudomonas aeruginosa" in FEMS Microbiology Letters, 246, no. 2 (2005):175-181,
https://doi.org/10.1016/j.femsle.2005.04.003 . .

TY  - JOUR
AU  - Bertani, I
AU  - Sevo, M
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2003
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/179
AB  - RpoS is the stationary phase sigma factor responsible for increased transcription of a set of genes when bacterial cells enter stationary phase and under stress conditions. In Escherichia coli, RpoS expression is modulated at the level of transcription, translation, and post-translational stability whereas in Pseudomonas, previous studies have implicated four genetic loci (psrA, gacA, lasI and rhlI) involved in rpoS transcription. In this report, the transcription, translation and proteins profiles of rpoS/RpoS were analyzed in response to growth phase of knockout genomic mutants in the P. aeruginosa transcriptional regulatory loci psrA, gacA, vfr, and in the las and rhl quorum-sensing systems. Gene expression and protein profiles were also analyzed in the ppk genomic mutant. This gene is responsible for the biosynthesis of polyphosphate, an alarmone involved in the regulation of RpoS accumulation in E. coli. Finally, the role of the ClpXP protease in RpoS regulation was also studied; in E. coli, this protease has been shown to rapidly degrade RpoS during exponential growth. These studies confirm the significant role of PsrA in rpoS transcription during the late-exponential and stationary growth phases, the probable role of Vfr in transcriptional repression during exponential phase, and the function of the ClpXP protease in RpoS degradation during exponential phase. GacA/GacS, the quorum-sensing systems, and the polyphosphate alarmone molecule were not significant in rpoS/RpoS regulation. These results demonstrate important similarities and differences with the regulation of this sigma factor in E. coli and in Pseudomonas.
PB  - Springer-Verlag, New York
T2  - Archives of Microbiology
T1  - Role of GacA, LasI, RhlI, ppk, PsrA, vfr and ClpXP in the regulation of the stationary-phase sigma factor rpoS/RpoS in Pseudomonas
EP  - 271
IS  - 4
SP  - 264
VL  - 180
DO  - 10.1007/s00203-003-0586-8
ER  - 

@article{
author = "Bertani, I and Sevo, M and Kojić, Milan and Venturi, V",
year = "2003",
abstract = "RpoS is the stationary phase sigma factor responsible for increased transcription of a set of genes when bacterial cells enter stationary phase and under stress conditions. In Escherichia coli, RpoS expression is modulated at the level of transcription, translation, and post-translational stability whereas in Pseudomonas, previous studies have implicated four genetic loci (psrA, gacA, lasI and rhlI) involved in rpoS transcription. In this report, the transcription, translation and proteins profiles of rpoS/RpoS were analyzed in response to growth phase of knockout genomic mutants in the P. aeruginosa transcriptional regulatory loci psrA, gacA, vfr, and in the las and rhl quorum-sensing systems. Gene expression and protein profiles were also analyzed in the ppk genomic mutant. This gene is responsible for the biosynthesis of polyphosphate, an alarmone involved in the regulation of RpoS accumulation in E. coli. Finally, the role of the ClpXP protease in RpoS regulation was also studied; in E. coli, this protease has been shown to rapidly degrade RpoS during exponential growth. These studies confirm the significant role of PsrA in rpoS transcription during the late-exponential and stationary growth phases, the probable role of Vfr in transcriptional repression during exponential phase, and the function of the ClpXP protease in RpoS degradation during exponential phase. GacA/GacS, the quorum-sensing systems, and the polyphosphate alarmone molecule were not significant in rpoS/RpoS regulation. These results demonstrate important similarities and differences with the regulation of this sigma factor in E. coli and in Pseudomonas.",
publisher = "Springer-Verlag, New York",
journal = "Archives of Microbiology",
title = "Role of GacA, LasI, RhlI, ppk, PsrA, vfr and ClpXP in the regulation of the stationary-phase sigma factor rpoS/RpoS in Pseudomonas",
pages = "271-264",
number = "4",
volume = "180",
doi = "10.1007/s00203-003-0586-8"
}

Bertani, I., Sevo, M., Kojić, M.,& Venturi, V.. (2003). Role of GacA, LasI, RhlI, ppk, PsrA, vfr and ClpXP in the regulation of the stationary-phase sigma factor rpoS/RpoS in Pseudomonas. in Archives of Microbiology
Springer-Verlag, New York., 180(4), 264-271.
https://doi.org/10.1007/s00203-003-0586-8

Bertani I, Sevo M, Kojić M, Venturi V. Role of GacA, LasI, RhlI, ppk, PsrA, vfr and ClpXP in the regulation of the stationary-phase sigma factor rpoS/RpoS in Pseudomonas. in Archives of Microbiology. 2003;180(4):264-271.
doi:10.1007/s00203-003-0586-8 .

Bertani, I, Sevo, M, Kojić, Milan, Venturi, V, "Role of GacA, LasI, RhlI, ppk, PsrA, vfr and ClpXP in the regulation of the stationary-phase sigma factor rpoS/RpoS in Pseudomonas" in Archives of Microbiology, 180, no. 4 (2003):264-271,
https://doi.org/10.1007/s00203-003-0586-8 . .

TY  - JOUR
AU  - Aguilar, C
AU  - Friscina, A
AU  - Devescovi, G
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2003
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/189
AB  - Quorum sensing is a regulatory mechanism (operating in response to cell density) which in gram-negative bacteria usually involves the production of N-acyl homoserine lactones (HSL). Quorum sensing in Burkholderia cepacia has been associated with the regulation of expression of extracellular proteins and siderophores and also with the regulation of swarming and biofilm formation. In the present study, several quorum-sensing-controlled gene promoters of B. cepacia ATCC 25416 were identified and characterized. A total of 28 putative gene promoters show CepR-C-8-HSL-dependent expression, suggesting that quorum sensing in B. cepacia is a global regulatory system.
PB  - Amer Soc Microbiology, Washington
T2  - Journal of Bacteriology
T1  - Identification of quorum-sensing-regulated genes of Burkholderia cepacia
EP  - 6462
IS  - 21
SP  - 6456
VL  - 185
DO  - 10.1128/JB.185.21.6456-6462.2003
ER  - 

@article{
author = "Aguilar, C and Friscina, A and Devescovi, G and Kojić, Milan and Venturi, V",
year = "2003",
abstract = "Quorum sensing is a regulatory mechanism (operating in response to cell density) which in gram-negative bacteria usually involves the production of N-acyl homoserine lactones (HSL). Quorum sensing in Burkholderia cepacia has been associated with the regulation of expression of extracellular proteins and siderophores and also with the regulation of swarming and biofilm formation. In the present study, several quorum-sensing-controlled gene promoters of B. cepacia ATCC 25416 were identified and characterized. A total of 28 putative gene promoters show CepR-C-8-HSL-dependent expression, suggesting that quorum sensing in B. cepacia is a global regulatory system.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Journal of Bacteriology",
title = "Identification of quorum-sensing-regulated genes of Burkholderia cepacia",
pages = "6462-6456",
number = "21",
volume = "185",
doi = "10.1128/JB.185.21.6456-6462.2003"
}

Aguilar, C., Friscina, A., Devescovi, G., Kojić, M.,& Venturi, V.. (2003). Identification of quorum-sensing-regulated genes of Burkholderia cepacia. in Journal of Bacteriology
Amer Soc Microbiology, Washington., 185(21), 6456-6462.
https://doi.org/10.1128/JB.185.21.6456-6462.2003

Aguilar C, Friscina A, Devescovi G, Kojić M, Venturi V. Identification of quorum-sensing-regulated genes of Burkholderia cepacia. in Journal of Bacteriology. 2003;185(21):6456-6462.
doi:10.1128/JB.185.21.6456-6462.2003 .

Aguilar, C, Friscina, A, Devescovi, G, Kojić, Milan, Venturi, V, "Identification of quorum-sensing-regulated genes of Burkholderia cepacia" in Journal of Bacteriology, 185, no. 21 (2003):6456-6462,
https://doi.org/10.1128/JB.185.21.6456-6462.2003 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Aguilar, C
AU  - Venturi, V
PY  - 2002
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/168
AB  - We have previously described a Pseudomonas gene, psrA, which enhances transcription of the rpoS sigma factor gene at stationary phase. We present molecular data which demonstrate that in Pseudomonas putida PsrA binds specifically to the rpoS and psrA promoters in DNA regions having similar palindromic sequences, C/GAAAC N2-4 GTTTG/C, where N is any nucleotide. The position of the initiation of transcription was determined for both promoters, and PsrA binds from positions - 59 to -35 in the rpoS promoter and from - 18 to + 20 in the psrA promoter with respect to the +1 transcription site. Expression studies with a psrA-lacZ transcriptional fusion in wild-type and psrA::Tn5 knockout mutants revealed that psrA was under additional control in response to growth phase. A model for the role of PsrA in the regulation of rpoS and psrA is presented.
PB  - Amer Soc Microbiology, Washington
T2  - Journal of Bacteriology
T1  - TetR family member PsrA directly binds the Pseudomonas rpoS and psrA promoters
EP  - 2330
IS  - 8
SP  - 2324
VL  - 184
DO  - 10.1128/JB.184.8.2324-2330.2002
ER  - 

@article{
author = "Kojić, Milan and Aguilar, C and Venturi, V",
year = "2002",
abstract = "We have previously described a Pseudomonas gene, psrA, which enhances transcription of the rpoS sigma factor gene at stationary phase. We present molecular data which demonstrate that in Pseudomonas putida PsrA binds specifically to the rpoS and psrA promoters in DNA regions having similar palindromic sequences, C/GAAAC N2-4 GTTTG/C, where N is any nucleotide. The position of the initiation of transcription was determined for both promoters, and PsrA binds from positions - 59 to -35 in the rpoS promoter and from - 18 to + 20 in the psrA promoter with respect to the +1 transcription site. Expression studies with a psrA-lacZ transcriptional fusion in wild-type and psrA::Tn5 knockout mutants revealed that psrA was under additional control in response to growth phase. A model for the role of PsrA in the regulation of rpoS and psrA is presented.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Journal of Bacteriology",
title = "TetR family member PsrA directly binds the Pseudomonas rpoS and psrA promoters",
pages = "2330-2324",
number = "8",
volume = "184",
doi = "10.1128/JB.184.8.2324-2330.2002"
}

Kojić, M., Aguilar, C.,& Venturi, V.. (2002). TetR family member PsrA directly binds the Pseudomonas rpoS and psrA promoters. in Journal of Bacteriology
Amer Soc Microbiology, Washington., 184(8), 2324-2330.
https://doi.org/10.1128/JB.184.8.2324-2330.2002

Kojić M, Aguilar C, Venturi V. TetR family member PsrA directly binds the Pseudomonas rpoS and psrA promoters. in Journal of Bacteriology. 2002;184(8):2324-2330.
doi:10.1128/JB.184.8.2324-2330.2002 .

Kojić, Milan, Aguilar, C, Venturi, V, "TetR family member PsrA directly binds the Pseudomonas rpoS and psrA promoters" in Journal of Bacteriology, 184, no. 8 (2002):2324-2330,
https://doi.org/10.1128/JB.184.8.2324-2330.2002 . .

TY  - JOUR
AU  - Bertani, I
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2001
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/158
AB  - The regulation of the p-hydroxybenzoate hydroxylase gene (pobA) of Pseudomonas putida WC5358 involved in the catabolism of p-hydroxybenzoic acid (PHB) to the central intermediate protocatechuate was studied. Protocatechuic acid (PCA) is then degraded via the beta -ketoadipate pathway to form tricarboxylic acid intermediates. In several Gram-negative bacteria pobA has been found genetically linked to a regulator called pobR which activates pobA expression in response to PHB, In this study the identification and characterization of the pobC-pobA locus of P, putida WCS358 is presented. The p-hydroxybenzoate hydroxylase (PobA) is highly identical to other identified PobA proteins, whereas the regulatory protein PobC did not display very high identity to other PobR proteins studied and belonged to the AraC family of regulatory proteins, hence it has been designated PobC, Using the pobA promoter transcriptionally fused to a promoterless lad gene it was observed that induction via PobC occurred very efficiently when PHB was present and to a lesser but still significant level also in the presence of PCA, This PobC-PCA response was genetically demonstrated by making use of pobC::Tn5 and pcaH::Tn5 mutants of strain WC5358 constructed in this study. In pobC mutants both the p-hydroxybenzoic and PCA response were not observed, whereas in the pcaH mutant, which lacks a functional protocatechuate 3,4-dioxygenase, the protocatechuic-acid-dependent pobA activation was still observed. Finally, the activation of pobA by PHB varied according to the concentration and it was observed that in the pcaR::Tn5 regulatory mutant of strain WCS358 the pobA promoter activity was reduced. PcaR is a regulator involved in the regulation of several loci of the beta -ketoadipate pathway, one of which is pcaK, It was postulated that the reduction of pobA activation in pcaR::Tn5 mutants was because there was no expression of the pcaK gene encoding the PHB transport protein resulting in lower levels of PHB present inside the cell.
PB  - Soc General Microbiology, Reading
T2  - Microbiology-Sgm
T1  - Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358
EP  - 1620
SP  - 1611
VL  - 147
DO  - 10.1099/00221287-147-6-1611
ER  - 

@article{
author = "Bertani, I and Kojić, Milan and Venturi, V",
year = "2001",
abstract = "The regulation of the p-hydroxybenzoate hydroxylase gene (pobA) of Pseudomonas putida WC5358 involved in the catabolism of p-hydroxybenzoic acid (PHB) to the central intermediate protocatechuate was studied. Protocatechuic acid (PCA) is then degraded via the beta -ketoadipate pathway to form tricarboxylic acid intermediates. In several Gram-negative bacteria pobA has been found genetically linked to a regulator called pobR which activates pobA expression in response to PHB, In this study the identification and characterization of the pobC-pobA locus of P, putida WCS358 is presented. The p-hydroxybenzoate hydroxylase (PobA) is highly identical to other identified PobA proteins, whereas the regulatory protein PobC did not display very high identity to other PobR proteins studied and belonged to the AraC family of regulatory proteins, hence it has been designated PobC, Using the pobA promoter transcriptionally fused to a promoterless lad gene it was observed that induction via PobC occurred very efficiently when PHB was present and to a lesser but still significant level also in the presence of PCA, This PobC-PCA response was genetically demonstrated by making use of pobC::Tn5 and pcaH::Tn5 mutants of strain WC5358 constructed in this study. In pobC mutants both the p-hydroxybenzoic and PCA response were not observed, whereas in the pcaH mutant, which lacks a functional protocatechuate 3,4-dioxygenase, the protocatechuic-acid-dependent pobA activation was still observed. Finally, the activation of pobA by PHB varied according to the concentration and it was observed that in the pcaR::Tn5 regulatory mutant of strain WCS358 the pobA promoter activity was reduced. PcaR is a regulator involved in the regulation of several loci of the beta -ketoadipate pathway, one of which is pcaK, It was postulated that the reduction of pobA activation in pcaR::Tn5 mutants was because there was no expression of the pcaK gene encoding the PHB transport protein resulting in lower levels of PHB present inside the cell.",
publisher = "Soc General Microbiology, Reading",
journal = "Microbiology-Sgm",
title = "Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358",
pages = "1620-1611",
volume = "147",
doi = "10.1099/00221287-147-6-1611"
}

Bertani, I., Kojić, M.,& Venturi, V.. (2001). Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358. in Microbiology-Sgm
Soc General Microbiology, Reading., 147, 1611-1620.
https://doi.org/10.1099/00221287-147-6-1611

Bertani I, Kojić M, Venturi V. Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358. in Microbiology-Sgm. 2001;147:1611-1620.
doi:10.1099/00221287-147-6-1611 .

Bertani, I, Kojić, Milan, Venturi, V, "Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358" in Microbiology-Sgm, 147 (2001):1611-1620,
https://doi.org/10.1099/00221287-147-6-1611 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2001
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/157
AB  - The rpoS gene encodes the sigma factor which was identified in several gram-negative bacteria as a central regulator during stationary phase. rpoS gene regulation is known to respond to cell density, showing higher expression in stationary phase. For Pseudomonas aeruginosa, it has been demonstrated that the cell-density dependent regulation response known as quorum sensing interacts with this regulatory response. Using the rpoS promoter of P. putida, we identified a genomic Tn5 insertion mutant of P. putida which showed a 90% decrease in rpoS promoter activity, resulting in less RpoS being present in a cell at stationary phase. Molecular analysis revealed that this mutant carried a Tn5 insertion in a gene, designated psrA (Pseudomonas sigma regulator), which codes for a protein (PsrA) of 26.3 kDa. PsrA contains a helix-turn-helix motif typical of DNA binding proteins and belongs to the TetR family of bacterial regulators. The homolog of the psrA gene was identified in P. aeruginosa; the protein showed 90% identity to PsrA of P. putida. A psrA::Tn5 insertion mutant of P, aeruginosa was constructed, In both Pseudomonas species, psrA was genetically linked to the SOS lexA repressor gene. Similar to what was observed for P. putida, a psrA null mutant of P. aeruginosa also showed a 90% reduction in rpoS promoter activity; both mutants could be complemented for rpoS promoter activity when the psrA gene was provided in trans, psrA mutants of both Pseudomonas species lost the ability to induce rpoS expression at stationary phase, but they retained the ability to produce quorum-sensing autoinducer molecules. PsrA was demonstrated to negatively regulate psrA gene expression in Pseudomonas and in Escherichia coli as well as to be capable of activating the rpoS promoter in E. call. Our data suggest that PsrA is an important regulatory protein of Pseudomonas spp. involved in the regulatory cascade controlling rpoS gene regulation in response to tell density.
PB  - Amer Soc Microbiology, Washington
T2  - Journal of Bacteriology
T1  - Regulation of rpoS gene expression in Pseudomonas: involvement of a TetR family regulator
EP  - 3720
IS  - 12
SP  - 3712
VL  - 183
DO  - 10.1128/JB.183.12.3712-3720.2001
ER  - 

@article{
author = "Kojić, Milan and Venturi, V",
year = "2001",
abstract = "The rpoS gene encodes the sigma factor which was identified in several gram-negative bacteria as a central regulator during stationary phase. rpoS gene regulation is known to respond to cell density, showing higher expression in stationary phase. For Pseudomonas aeruginosa, it has been demonstrated that the cell-density dependent regulation response known as quorum sensing interacts with this regulatory response. Using the rpoS promoter of P. putida, we identified a genomic Tn5 insertion mutant of P. putida which showed a 90% decrease in rpoS promoter activity, resulting in less RpoS being present in a cell at stationary phase. Molecular analysis revealed that this mutant carried a Tn5 insertion in a gene, designated psrA (Pseudomonas sigma regulator), which codes for a protein (PsrA) of 26.3 kDa. PsrA contains a helix-turn-helix motif typical of DNA binding proteins and belongs to the TetR family of bacterial regulators. The homolog of the psrA gene was identified in P. aeruginosa; the protein showed 90% identity to PsrA of P. putida. A psrA::Tn5 insertion mutant of P, aeruginosa was constructed, In both Pseudomonas species, psrA was genetically linked to the SOS lexA repressor gene. Similar to what was observed for P. putida, a psrA null mutant of P. aeruginosa also showed a 90% reduction in rpoS promoter activity; both mutants could be complemented for rpoS promoter activity when the psrA gene was provided in trans, psrA mutants of both Pseudomonas species lost the ability to induce rpoS expression at stationary phase, but they retained the ability to produce quorum-sensing autoinducer molecules. PsrA was demonstrated to negatively regulate psrA gene expression in Pseudomonas and in Escherichia coli as well as to be capable of activating the rpoS promoter in E. call. Our data suggest that PsrA is an important regulatory protein of Pseudomonas spp. involved in the regulatory cascade controlling rpoS gene regulation in response to tell density.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Journal of Bacteriology",
title = "Regulation of rpoS gene expression in Pseudomonas: involvement of a TetR family regulator",
pages = "3720-3712",
number = "12",
volume = "183",
doi = "10.1128/JB.183.12.3712-3720.2001"
}

Kojić, M.,& Venturi, V.. (2001). Regulation of rpoS gene expression in Pseudomonas: involvement of a TetR family regulator. in Journal of Bacteriology
Amer Soc Microbiology, Washington., 183(12), 3712-3720.
https://doi.org/10.1128/JB.183.12.3712-3720.2001

Kojić M, Venturi V. Regulation of rpoS gene expression in Pseudomonas: involvement of a TetR family regulator. in Journal of Bacteriology. 2001;183(12):3712-3720.
doi:10.1128/JB.183.12.3712-3720.2001 .

Kojić, Milan, Venturi, V, "Regulation of rpoS gene expression in Pseudomonas: involvement of a TetR family regulator" in Journal of Bacteriology, 183, no. 12 (2001):3712-3720,
https://doi.org/10.1128/JB.183.12.3712-3720.2001 . .

TY  - JOUR
AU  - Degrassi, G
AU  - Kojić, Milan
AU  - Ljubijankić, G
AU  - Venturi, V
PY  - 2000
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/140
AB  - The Bacillus pumilus gene encoding acetyl xylan esterase tare) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar sire and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.
PB  - Microbiology Soc, London
T2  - Microbiology-Sgm
T1  - The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity
EP  - 1591
SP  - 1585
VL  - 146
DO  - 10.1099/00221287-146-7-1585
ER  - 

@article{
author = "Degrassi, G and Kojić, Milan and Ljubijankić, G and Venturi, V",
year = "2000",
abstract = "The Bacillus pumilus gene encoding acetyl xylan esterase tare) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar sire and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.",
publisher = "Microbiology Soc, London",
journal = "Microbiology-Sgm",
title = "The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity",
pages = "1591-1585",
volume = "146",
doi = "10.1099/00221287-146-7-1585"
}

Degrassi, G., Kojić, M., Ljubijankić, G.,& Venturi, V.. (2000). The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. in Microbiology-Sgm
Microbiology Soc, London., 146, 1585-1591.
https://doi.org/10.1099/00221287-146-7-1585

Degrassi G, Kojić M, Ljubijankić G, Venturi V. The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. in Microbiology-Sgm. 2000;146:1585-1591.
doi:10.1099/00221287-146-7-1585 .

Degrassi, G, Kojić, Milan, Ljubijankić, G, Venturi, V, "The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity" in Microbiology-Sgm, 146 (2000):1585-1591,
https://doi.org/10.1099/00221287-146-7-1585 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Degrassi, G
AU  - Venturi, V
PY  - 1999
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/127
AB  - The rpoS gene which encodes a stationary phase sigma factor has been identified and characterised from the rhizosphere-colonising plant growth-promoting Pseudomonas putida strain WCS358. The predicted protein sequence has extensive homologies with the RpoS proteins form other bacteria, in particular with the RpoS sigma factors of the fluorescent pseudomonads. A genomic transposon insertion in the rpoS gene was constructed, these mutants were analysed for their ability to produce siderophore (iron-transport agent) and the autoinducer quorum-sensing molecules called homoserine lactones (AHL). It was determined that RpoS was not involved in the regulation of siderophore and AHL production, synthesis of these molecules is important for gene expression at stationary phase. P. putida WCS358 produces at least three different AHL molecules.
PB  - Elsevier, Amsterdam
T2  - Biochimica Et Biophysica Acta-Gene Structure and Expression
T1  - Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production
EP  - 420
IS  - 2-3
SP  - 413
VL  - 1489
DO  - 10.1016/S0167-4781(99)00210-9
ER  - 

@article{
author = "Kojić, Milan and Degrassi, G and Venturi, V",
year = "1999",
abstract = "The rpoS gene which encodes a stationary phase sigma factor has been identified and characterised from the rhizosphere-colonising plant growth-promoting Pseudomonas putida strain WCS358. The predicted protein sequence has extensive homologies with the RpoS proteins form other bacteria, in particular with the RpoS sigma factors of the fluorescent pseudomonads. A genomic transposon insertion in the rpoS gene was constructed, these mutants were analysed for their ability to produce siderophore (iron-transport agent) and the autoinducer quorum-sensing molecules called homoserine lactones (AHL). It was determined that RpoS was not involved in the regulation of siderophore and AHL production, synthesis of these molecules is important for gene expression at stationary phase. P. putida WCS358 produces at least three different AHL molecules.",
publisher = "Elsevier, Amsterdam",
journal = "Biochimica Et Biophysica Acta-Gene Structure and Expression",
title = "Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production",
pages = "420-413",
number = "2-3",
volume = "1489",
doi = "10.1016/S0167-4781(99)00210-9"
}

Kojić, M., Degrassi, G.,& Venturi, V.. (1999). Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production. in Biochimica Et Biophysica Acta-Gene Structure and Expression
Elsevier, Amsterdam., 1489(2-3), 413-420.
https://doi.org/10.1016/S0167-4781(99)00210-9

Kojić M, Degrassi G, Venturi V. Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production. in Biochimica Et Biophysica Acta-Gene Structure and Expression. 1999;1489(2-3):413-420.
doi:10.1016/S0167-4781(99)00210-9 .

Kojić, Milan, Degrassi, G, Venturi, V, "Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production" in Biochimica Et Biophysica Acta-Gene Structure and Expression, 1489, no. 2-3 (1999):413-420,
https://doi.org/10.1016/S0167-4781(99)00210-9 . .