TY  - JOUR
AU  - Stodulkova, Eva
AU  - Kuzma, Marek
AU  - Hench, Ivana Bratic
AU  - Cerny, Jan
AU  - Kralova, Jarmila
AU  - Novak, Petr
AU  - Chudickova, Milada
AU  - Savić, Miloje
AU  - Đokić, Lidija
AU  - Vasiljević, Branka
AU  - Flieger, Miroslav
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/492
AB  - A new polyene macrolide family, closely related to the pentaene macrolide antibiotic roflamycoin, was isolated from the both fermentation broth and biomass of Streptomyces durmitorensis wild-type strain MS405. The main compound was identified by NMR and Fourier transform ion cyclotron resonance mass spectrometry as 32,33-didehydroroflamycoin (1; DDHR). Additional four structurally related compounds were determined solely by MS analysis. DDHR induces cell death by apoptosis in various cancer cell lines as demonstrated by DNA fragmentation. Striking feature of DDHR is its internal fluorescence allowing visualization of labeled plasma membranes and internal membrane structures. The Journal of Antibiotics (2011) 64, 717-722; doi:10.1038/ja.2011.81; published online 14 September 2011
PB  - Nature Publishing Group, London
T2  - Journal of Antibiotics
T1  - New polyene macrolide family produced by submerged culture of Streptomyces durmitorensis
EP  - 722
IS  - 11
SP  - 717
VL  - 64
DO  - 10.1038/ja.2011.81
ER  - 

@article{
author = "Stodulkova, Eva and Kuzma, Marek and Hench, Ivana Bratic and Cerny, Jan and Kralova, Jarmila and Novak, Petr and Chudickova, Milada and Savić, Miloje and Đokić, Lidija and Vasiljević, Branka and Flieger, Miroslav",
year = "2011",
abstract = "A new polyene macrolide family, closely related to the pentaene macrolide antibiotic roflamycoin, was isolated from the both fermentation broth and biomass of Streptomyces durmitorensis wild-type strain MS405. The main compound was identified by NMR and Fourier transform ion cyclotron resonance mass spectrometry as 32,33-didehydroroflamycoin (1; DDHR). Additional four structurally related compounds were determined solely by MS analysis. DDHR induces cell death by apoptosis in various cancer cell lines as demonstrated by DNA fragmentation. Striking feature of DDHR is its internal fluorescence allowing visualization of labeled plasma membranes and internal membrane structures. The Journal of Antibiotics (2011) 64, 717-722; doi:10.1038/ja.2011.81; published online 14 September 2011",
publisher = "Nature Publishing Group, London",
journal = "Journal of Antibiotics",
title = "New polyene macrolide family produced by submerged culture of Streptomyces durmitorensis",
pages = "722-717",
number = "11",
volume = "64",
doi = "10.1038/ja.2011.81"
}

Stodulkova, E., Kuzma, M., Hench, I. B., Cerny, J., Kralova, J., Novak, P., Chudickova, M., Savić, M., Đokić, L., Vasiljević, B.,& Flieger, M.. (2011). New polyene macrolide family produced by submerged culture of Streptomyces durmitorensis. in Journal of Antibiotics
Nature Publishing Group, London., 64(11), 717-722.
https://doi.org/10.1038/ja.2011.81

Stodulkova E, Kuzma M, Hench IB, Cerny J, Kralova J, Novak P, Chudickova M, Savić M, Đokić L, Vasiljević B, Flieger M. New polyene macrolide family produced by submerged culture of Streptomyces durmitorensis. in Journal of Antibiotics. 2011;64(11):717-722.
doi:10.1038/ja.2011.81 .

Stodulkova, Eva, Kuzma, Marek, Hench, Ivana Bratic, Cerny, Jan, Kralova, Jarmila, Novak, Petr, Chudickova, Milada, Savić, Miloje, Đokić, Lidija, Vasiljević, Branka, Flieger, Miroslav, "New polyene macrolide family produced by submerged culture of Streptomyces durmitorensis" in Journal of Antibiotics, 64, no. 11 (2011):717-722,
https://doi.org/10.1038/ja.2011.81 . .

TY  - JOUR
AU  - Vojnović, Sandra
AU  - Ilić-Tomić, Tatjana
AU  - Morić, Ivana
AU  - Vasiljević, Branka
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/449
AB  - Sgm metiltransferaza iz soja Micromonospora zionensis i KgmB metiltransferaza iz soja Streptoalloteichus tenebrarius ostvaruju rezistenciju na aminoglikozidne antibiotike metilacijom nukleotida na poziciji G1405 u okviru A mesta na 16S rRNK. Smatra se da je za autoregulaciju sgm gena odgovoran (C)CCGCCC motiv. Najverovatnije je ista sekvenca odgovorna i za autoregulaciju kgmB gena. Po kompjuterskoj predikciji, ovaj motiv, lociran u 5' netranslatirajućem regionu iRNK molekula oba gena, bi mogao učestvovati u formiranju sekundarne strukture tipa ukosnice. Kako Sgm i KgmB metiltransferaze jedna drugu autoregulišu, moguće je da prepoznaju iste cis elemente u iRNK molekulima. Eksperimenti ispitivanja strukture su, s jedne strane potvrdili prisustvo stabilne sekundarne strukture u okviru 5' netranslatirajućeg regiona iRNK molekula sgm gena, a sa druge, nisu dokazali postojanje modelovane sekundarne strukture u iRNK molekulu kgmB gena.
AB  - Sgm methyltransferase from Micromonospora zionensis and KgmB methyltransferase from Streptoalloteichus tenebrarius are resistant to aminoglycoside antibiotics as a result of their ability to specifically methylate G1405 within the bacterial 16S rRNA A-site. The (C)CGCCC motif, assumed to be a regulatory sequence responsible for the autoregulation of the sgm gene, could most likely also be responsible for the autoregulation of the kgmB gene. This sequence, found within the 5' untranslated region of both sgm and kgmB mRNAs, as indicated by in silico prediction, may be involved in the formation of a specific stem-loop structure. Sgm and KgmB are mutually down-regulated and it is likely that they share the same cis-acting elements. Structure probing experiments confirmed the existence of a stable secondary structure within the 5' UTR of the sgm mRNA, while the analysis of kgmB mRNA failed to confirm the predicted structure.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Analiza sekundarne strukture u okviru sgm i kgmB mRNA
T1  - Analysis of secondary structure within sgm and kgmB mRNA
EP  - 524
IS  - 3
SP  - 515
VL  - 62
DO  - 10.2298/ABS1003515V
ER  - 

@article{
author = "Vojnović, Sandra and Ilić-Tomić, Tatjana and Morić, Ivana and Vasiljević, Branka",
year = "2010",
abstract = "Sgm metiltransferaza iz soja Micromonospora zionensis i KgmB metiltransferaza iz soja Streptoalloteichus tenebrarius ostvaruju rezistenciju na aminoglikozidne antibiotike metilacijom nukleotida na poziciji G1405 u okviru A mesta na 16S rRNK. Smatra se da je za autoregulaciju sgm gena odgovoran (C)CCGCCC motiv. Najverovatnije je ista sekvenca odgovorna i za autoregulaciju kgmB gena. Po kompjuterskoj predikciji, ovaj motiv, lociran u 5' netranslatirajućem regionu iRNK molekula oba gena, bi mogao učestvovati u formiranju sekundarne strukture tipa ukosnice. Kako Sgm i KgmB metiltransferaze jedna drugu autoregulišu, moguće je da prepoznaju iste cis elemente u iRNK molekulima. Eksperimenti ispitivanja strukture su, s jedne strane potvrdili prisustvo stabilne sekundarne strukture u okviru 5' netranslatirajućeg regiona iRNK molekula sgm gena, a sa druge, nisu dokazali postojanje modelovane sekundarne strukture u iRNK molekulu kgmB gena., Sgm methyltransferase from Micromonospora zionensis and KgmB methyltransferase from Streptoalloteichus tenebrarius are resistant to aminoglycoside antibiotics as a result of their ability to specifically methylate G1405 within the bacterial 16S rRNA A-site. The (C)CGCCC motif, assumed to be a regulatory sequence responsible for the autoregulation of the sgm gene, could most likely also be responsible for the autoregulation of the kgmB gene. This sequence, found within the 5' untranslated region of both sgm and kgmB mRNAs, as indicated by in silico prediction, may be involved in the formation of a specific stem-loop structure. Sgm and KgmB are mutually down-regulated and it is likely that they share the same cis-acting elements. Structure probing experiments confirmed the existence of a stable secondary structure within the 5' UTR of the sgm mRNA, while the analysis of kgmB mRNA failed to confirm the predicted structure.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Analiza sekundarne strukture u okviru sgm i kgmB mRNA, Analysis of secondary structure within sgm and kgmB mRNA",
pages = "524-515",
number = "3",
volume = "62",
doi = "10.2298/ABS1003515V"
}

Vojnović, S., Ilić-Tomić, T., Morić, I.,& Vasiljević, B.. (2010). Analiza sekundarne strukture u okviru sgm i kgmB mRNA. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 62(3), 515-524.
https://doi.org/10.2298/ABS1003515V

Vojnović S, Ilić-Tomić T, Morić I, Vasiljević B. Analiza sekundarne strukture u okviru sgm i kgmB mRNA. in Archives of Biological Sciences. 2010;62(3):515-524.
doi:10.2298/ABS1003515V .

Vojnović, Sandra, Ilić-Tomić, Tatjana, Morić, Ivana, Vasiljević, Branka, "Analiza sekundarne strukture u okviru sgm i kgmB mRNA" in Archives of Biological Sciences, 62, no. 3 (2010):515-524,
https://doi.org/10.2298/ABS1003515V . .

TY  - JOUR
AU  - Morić, Ivana
AU  - Savić, Miloje
AU  - Ilić-Tomić, Tatjana
AU  - Vojnović, Sandra
AU  - Bajkić, Sanja
AU  - Vasiljević, Branka
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/455
AB  - Metiltransferaze (MTaze), koje čine veliku proteinsku superfamiliju, kao donatora metil grupe najčešće koriste S-adenozil-L-metionin (SAM). SAM-zavisne MTaze metiluju nukleinske kiseline (DNK, RNK) i proteine, modulišući tako njihovu aktivnost, funkciju i strukturnu organizaciju. Metilacija G1405 ili A1408 baza u 16S rRNK mikroorganizama koji proizvode aminoglikozide obezbeđuje rezistenciju na sopstvene toksične proizvode. Ovaj mehanizam rezistencije je donedavno bio opisan samo kod proizvođača antibiotika. Od 2003. godine i kod patogenih bakterija beleži se neprestan porast rezistencije na aminoglikozide putem ovog mehanizma, što predstavlja veliku pretnju efikasnoj upotrebi aminoglikozida u kliničkoj praksi. Jedno od mogućih rešenja problema leži u razvoju novih jedinjenja koja bi efikasno delovala na nova mesta u okviru ribozoma. Drugi pristup rešavanju ovog problema uključuje razvoj inhibitora MTaza odgovornih za rezistenciju, sa idejom da se onemogući modifikacija bakterijske rRNK i na taj način vrati terapeutska efikasnost postojećim aminoglikozidima. Fundamentalna istraživanja vezana za proteinsku ekspresiju, potpuno razumevanje mehanizma rezistencije kao i razrešenje tercijarne strukture proteina su neophodan preduslov za primenu inhibitora 16S rRNK MTaza u medicini.
AB  - Methyltransferases (MTases), a large protein superfamily, commonly use S-adenosyl-L-methionine (SAM) as the methyl group donor. SAM-dependant MTases methylate both nucleic acids (DNA, RNA) and proteins, and thus modulate their activity, function and folding. Methylation of G1405 or A1408 nucleotides of 16S rRNA in aminoglycoside-producing microorganisms confers the resistance to their own toxic product(s). This mechanism of resistance has been considered as unique to antibiotics producers until recently. Since 2003, methylation of 16S rRNA as a mechanism of resistance is increasingly emerging in pathogenic bacteria. This represents a major threat towards the usefulness of aminoglycosides in the clinical practice. A potential solution to the problem involves the design of novel compounds that would act against new ribosomal targets. The second approach to the issue includes the development of resistance MTases' inhibitors, with the idea to prevent them from modifying the bacterial rRNA, and thus reinstate the therapeutic power of existing aminoglycosides. As the latter approach has considerable potential, it is obvious that fundamental research related to protein expression, in-depth understanding of the mechanism of action and resolving a tertiary structure of 16S rRNAs MTases are prerequisites for application in medicine.
PB  - Društvo medicinskih biohemičara Srbije, Beograd i Versita
T2  - Journal of Medical Biochemistry
T1  - rRNK metiltransferaze i njihova uloga u rezistenciji na antibiotike
T1  - rRNA methyltransferases and their role in resistance to antibiotics
EP  - 174
IS  - 3
SP  - 165
VL  - 29
DO  - 10.2478/v10011-010-0030-y
ER  - 

@article{
author = "Morić, Ivana and Savić, Miloje and Ilić-Tomić, Tatjana and Vojnović, Sandra and Bajkić, Sanja and Vasiljević, Branka",
year = "2010",
abstract = "Metiltransferaze (MTaze), koje čine veliku proteinsku superfamiliju, kao donatora metil grupe najčešće koriste S-adenozil-L-metionin (SAM). SAM-zavisne MTaze metiluju nukleinske kiseline (DNK, RNK) i proteine, modulišući tako njihovu aktivnost, funkciju i strukturnu organizaciju. Metilacija G1405 ili A1408 baza u 16S rRNK mikroorganizama koji proizvode aminoglikozide obezbeđuje rezistenciju na sopstvene toksične proizvode. Ovaj mehanizam rezistencije je donedavno bio opisan samo kod proizvođača antibiotika. Od 2003. godine i kod patogenih bakterija beleži se neprestan porast rezistencije na aminoglikozide putem ovog mehanizma, što predstavlja veliku pretnju efikasnoj upotrebi aminoglikozida u kliničkoj praksi. Jedno od mogućih rešenja problema leži u razvoju novih jedinjenja koja bi efikasno delovala na nova mesta u okviru ribozoma. Drugi pristup rešavanju ovog problema uključuje razvoj inhibitora MTaza odgovornih za rezistenciju, sa idejom da se onemogući modifikacija bakterijske rRNK i na taj način vrati terapeutska efikasnost postojećim aminoglikozidima. Fundamentalna istraživanja vezana za proteinsku ekspresiju, potpuno razumevanje mehanizma rezistencije kao i razrešenje tercijarne strukture proteina su neophodan preduslov za primenu inhibitora 16S rRNK MTaza u medicini., Methyltransferases (MTases), a large protein superfamily, commonly use S-adenosyl-L-methionine (SAM) as the methyl group donor. SAM-dependant MTases methylate both nucleic acids (DNA, RNA) and proteins, and thus modulate their activity, function and folding. Methylation of G1405 or A1408 nucleotides of 16S rRNA in aminoglycoside-producing microorganisms confers the resistance to their own toxic product(s). This mechanism of resistance has been considered as unique to antibiotics producers until recently. Since 2003, methylation of 16S rRNA as a mechanism of resistance is increasingly emerging in pathogenic bacteria. This represents a major threat towards the usefulness of aminoglycosides in the clinical practice. A potential solution to the problem involves the design of novel compounds that would act against new ribosomal targets. The second approach to the issue includes the development of resistance MTases' inhibitors, with the idea to prevent them from modifying the bacterial rRNA, and thus reinstate the therapeutic power of existing aminoglycosides. As the latter approach has considerable potential, it is obvious that fundamental research related to protein expression, in-depth understanding of the mechanism of action and resolving a tertiary structure of 16S rRNAs MTases are prerequisites for application in medicine.",
publisher = "Društvo medicinskih biohemičara Srbije, Beograd i Versita",
journal = "Journal of Medical Biochemistry",
title = "rRNK metiltransferaze i njihova uloga u rezistenciji na antibiotike, rRNA methyltransferases and their role in resistance to antibiotics",
pages = "174-165",
number = "3",
volume = "29",
doi = "10.2478/v10011-010-0030-y"
}

Morić, I., Savić, M., Ilić-Tomić, T., Vojnović, S., Bajkić, S.,& Vasiljević, B.. (2010). rRNK metiltransferaze i njihova uloga u rezistenciji na antibiotike. in Journal of Medical Biochemistry
Društvo medicinskih biohemičara Srbije, Beograd i Versita., 29(3), 165-174.
https://doi.org/10.2478/v10011-010-0030-y

Morić I, Savić M, Ilić-Tomić T, Vojnović S, Bajkić S, Vasiljević B. rRNK metiltransferaze i njihova uloga u rezistenciji na antibiotike. in Journal of Medical Biochemistry. 2010;29(3):165-174.
doi:10.2478/v10011-010-0030-y .

Morić, Ivana, Savić, Miloje, Ilić-Tomić, Tatjana, Vojnović, Sandra, Bajkić, Sanja, Vasiljević, Branka, "rRNK metiltransferaze i njihova uloga u rezistenciji na antibiotike" in Journal of Medical Biochemistry, 29, no. 3 (2010):165-174,
https://doi.org/10.2478/v10011-010-0030-y . .

TY  - JOUR
AU  - Đokić, Lidija
AU  - Savić, M.
AU  - Narančić, Tanja
AU  - Vasiljević, Branka
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/447
AB  - Ramonda serbica i Ramonda nathaliae, retke biljke 'vaskrsnice' koje rastu na Balkanskom poluostrvu, u odgovoru na stres produkuju velike količine fenola. Bakterijske zajednice poreklom iz rizosfere ovih biljaka analizirane su metagenomskim pristupom. Fluorescentna 'in situ' hibridizacija (FISH) i DAPI bojenje pokazali su da u analiziranim zemljištima ima svega 5% metabolički aktivnih bakterija. Upotrebom prajmera specifičnih za bakterijsku DNK umnoženi su geni za 16S rDNK i konstruisane su dve genske biblioteke. Biblioteke su pretraživane uz pomoć RFLP metode. Od ukupno 192 klona dobijena iz uzorka rizosfere R. nathaliae identifikovano je 35 operativnih taksonomskih jedinica (OTJ), dok je iz uzorka rizosfere R. serbica dobijeno 13 OTJ od ukupno 80 klonova. Predstavnici svake OTJ su sekvencirani. Analizirane zajednice odlikuje veoma mali diverzitet i većina dobijenih sekvenci je pokazala malu sličnost sa DNK sekvencama do sada kultivisanih bakterija.
AB  - Ramonda serbica and Ramonda nathaliae, rare resurrection plants growing in the Balkan Peninsula, produce a high amount of phenolic compounds as a response to stress. The composition and size of bacterial communities in two rhizosphere soil samples of these plants were analyzed using a metagenomic approach. Fluorescent in situ hybridization (FISH) experiments together with DAPI staining showed that the metabolically active bacteria represent only a small fraction, approximately 5%, of total soil bacteria. Using universal bacteria - specific primers 16S rDNA genes were amplified directly from metagenomic DNAs and two libraries were constructed. The Restriction Fragment Length Polymorphism (RLFP) method was used in library screening. Amongst 192 clones, 35 unique operational taxonomic units (OTUs) were determined from the rhizosphere of R. nathaliae, and 13 OTUs out of 80 clones in total from the library of R. serbica. Representative clones from each OTU were sequenced. The majority of sequences from metagenomes showed very little similarity to any cultured bacteria. In conclusion, the bacterial communities in the studied soil samples showed quite poor diversity.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Metagenomska analiza zemljišnih mikrobioloških zajednica
T1  - Metagenomic analysis of soil microbial communities
EP  - 564
IS  - 3
SP  - 559
VL  - 62
DO  - 10.2298/ABS1003559D
ER  - 

@article{
author = "Đokić, Lidija and Savić, M. and Narančić, Tanja and Vasiljević, Branka",
year = "2010",
abstract = "Ramonda serbica i Ramonda nathaliae, retke biljke 'vaskrsnice' koje rastu na Balkanskom poluostrvu, u odgovoru na stres produkuju velike količine fenola. Bakterijske zajednice poreklom iz rizosfere ovih biljaka analizirane su metagenomskim pristupom. Fluorescentna 'in situ' hibridizacija (FISH) i DAPI bojenje pokazali su da u analiziranim zemljištima ima svega 5% metabolički aktivnih bakterija. Upotrebom prajmera specifičnih za bakterijsku DNK umnoženi su geni za 16S rDNK i konstruisane su dve genske biblioteke. Biblioteke su pretraživane uz pomoć RFLP metode. Od ukupno 192 klona dobijena iz uzorka rizosfere R. nathaliae identifikovano je 35 operativnih taksonomskih jedinica (OTJ), dok je iz uzorka rizosfere R. serbica dobijeno 13 OTJ od ukupno 80 klonova. Predstavnici svake OTJ su sekvencirani. Analizirane zajednice odlikuje veoma mali diverzitet i većina dobijenih sekvenci je pokazala malu sličnost sa DNK sekvencama do sada kultivisanih bakterija., Ramonda serbica and Ramonda nathaliae, rare resurrection plants growing in the Balkan Peninsula, produce a high amount of phenolic compounds as a response to stress. The composition and size of bacterial communities in two rhizosphere soil samples of these plants were analyzed using a metagenomic approach. Fluorescent in situ hybridization (FISH) experiments together with DAPI staining showed that the metabolically active bacteria represent only a small fraction, approximately 5%, of total soil bacteria. Using universal bacteria - specific primers 16S rDNA genes were amplified directly from metagenomic DNAs and two libraries were constructed. The Restriction Fragment Length Polymorphism (RLFP) method was used in library screening. Amongst 192 clones, 35 unique operational taxonomic units (OTUs) were determined from the rhizosphere of R. nathaliae, and 13 OTUs out of 80 clones in total from the library of R. serbica. Representative clones from each OTU were sequenced. The majority of sequences from metagenomes showed very little similarity to any cultured bacteria. In conclusion, the bacterial communities in the studied soil samples showed quite poor diversity.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Metagenomska analiza zemljišnih mikrobioloških zajednica, Metagenomic analysis of soil microbial communities",
pages = "564-559",
number = "3",
volume = "62",
doi = "10.2298/ABS1003559D"
}

Đokić, L., Savić, M., Narančić, T.,& Vasiljević, B.. (2010). Metagenomska analiza zemljišnih mikrobioloških zajednica. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 62(3), 559-564.
https://doi.org/10.2298/ABS1003559D

Đokić L, Savić M, Narančić T, Vasiljević B. Metagenomska analiza zemljišnih mikrobioloških zajednica. in Archives of Biological Sciences. 2010;62(3):559-564.
doi:10.2298/ABS1003559D .

Đokić, Lidija, Savić, M., Narančić, Tanja, Vasiljević, Branka, "Metagenomska analiza zemljišnih mikrobioloških zajednica" in Archives of Biological Sciences, 62, no. 3 (2010):559-564,
https://doi.org/10.2298/ABS1003559D . .

TY  - JOUR
AU  - Morić, Ivana
AU  - Jeremić, Sanja
AU  - Savić, Miloje
AU  - Ilić-Tomić, Tatjana
AU  - Conn, Graeme L.
AU  - Vasiljević, Branka
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/374
AB  - The mechanism of resistance to aminoglycosides based on methylation of their target, 16S rRNA, was until recently described only in antibiotic producing microorganisms. However, equivalent methyltransferases have now also been identified among numerous clinical Gram-negative pathogenic isolates. We have cloned, expressed, and purified GrmA, the aminoglycoside-resistance methyltransferase from Micromonospora purpurea, producer of gentamicin complex. Two vectors were created that express protein with an N-terminal 6x histidine tag with and without an enterokinase recognition producing proteins His(6)-EK-GrmA and His(6)-GrmA, respectively. The activity of both recombinant proteins was demonstrated in vivo. After optimized expression and native purification both protein variants proved to be active in in vitro methylation assays. This work lays a foundation for future detailed biochemical, structural and pharmacological studies with this member of an important group of aminoglycoside-resistance enzymes.
PB  - Springer, New York
T2  - Protein Journal
T1  - Heterologous Escherichia coli Expression, Purification and Characterization of the GrmA Aminoglycoside-Resistance Methyltransferase
EP  - 332
IS  - 7-8
SP  - 326
VL  - 28
DO  - 10.1007/s10930-009-9197-9
ER  - 

@article{
author = "Morić, Ivana and Jeremić, Sanja and Savić, Miloje and Ilić-Tomić, Tatjana and Conn, Graeme L. and Vasiljević, Branka",
year = "2009",
abstract = "The mechanism of resistance to aminoglycosides based on methylation of their target, 16S rRNA, was until recently described only in antibiotic producing microorganisms. However, equivalent methyltransferases have now also been identified among numerous clinical Gram-negative pathogenic isolates. We have cloned, expressed, and purified GrmA, the aminoglycoside-resistance methyltransferase from Micromonospora purpurea, producer of gentamicin complex. Two vectors were created that express protein with an N-terminal 6x histidine tag with and without an enterokinase recognition producing proteins His(6)-EK-GrmA and His(6)-GrmA, respectively. The activity of both recombinant proteins was demonstrated in vivo. After optimized expression and native purification both protein variants proved to be active in in vitro methylation assays. This work lays a foundation for future detailed biochemical, structural and pharmacological studies with this member of an important group of aminoglycoside-resistance enzymes.",
publisher = "Springer, New York",
journal = "Protein Journal",
title = "Heterologous Escherichia coli Expression, Purification and Characterization of the GrmA Aminoglycoside-Resistance Methyltransferase",
pages = "332-326",
number = "7-8",
volume = "28",
doi = "10.1007/s10930-009-9197-9"
}

Morić, I., Jeremić, S., Savić, M., Ilić-Tomić, T., Conn, G. L.,& Vasiljević, B.. (2009). Heterologous Escherichia coli Expression, Purification and Characterization of the GrmA Aminoglycoside-Resistance Methyltransferase. in Protein Journal
Springer, New York., 28(7-8), 326-332.
https://doi.org/10.1007/s10930-009-9197-9

Morić I, Jeremić S, Savić M, Ilić-Tomić T, Conn GL, Vasiljević B. Heterologous Escherichia coli Expression, Purification and Characterization of the GrmA Aminoglycoside-Resistance Methyltransferase. in Protein Journal. 2009;28(7-8):326-332.
doi:10.1007/s10930-009-9197-9 .

Morić, Ivana, Jeremić, Sanja, Savić, Miloje, Ilić-Tomić, Tatjana, Conn, Graeme L., Vasiljević, Branka, "Heterologous Escherichia coli Expression, Purification and Characterization of the GrmA Aminoglycoside-Resistance Methyltransferase" in Protein Journal, 28, no. 7-8 (2009):326-332,
https://doi.org/10.1007/s10930-009-9197-9 . .

TY  - JOUR
AU  - Šenerović, Lidija
AU  - Stanković, Nada
AU  - Ljubijankić, G.
AU  - Vasiljević, Branka
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/381
AB  - Penicilin G acilaza (PAC) je jedan od najšire korišćenih enzima u industrijskoj sintezi polusintetskih antibiotika. U ovom radu dobijeni nivo ekspresije PAC gena iz Providencia rettgeri u ekspresionom sistemu Pichia pastoris iznosio je 2.7 U/ml. Rekombinantni enzim je prečišćen i određen je njegov glikozilacioni status. Nađeno je da osim što su obe subjedinice enzima (α i β) N-glikozilovane, β subjedinica sadrži još i O-glikane. Takođe je ustanovljeno da je rekombinantna PACP. rett. stabilna u širokom pH opsegu što ju je, zajedno sa predhodno ustanovljenom visokom termostabilnošću, učinilo izuzetno privlačnim biokatalizatorom sa industrijske tačke gledišta.
AB  - Penicillin G acylase (PAC) is one of the most widely used enzymes in industrial synthesis of semi-synthetic antibiotics. The Providencia rettgeri pac gene was expressed to a level of 2.7 U/ml using the Pichia pastoris expression system. The recombinant enzyme was purified and its glycosylation status was determined. It was found that both subunits (α and β) of the enzyme were N-glycosylated, while the β-subunit also contained O-glycans. It was also observed that rPACP.rett. was stable in a wide range of pH, which, in addition to the previously proved high thermostability, makes it an attractive biocatalyst from an industrial point of view.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Glikozilacija i pH stabilnost penicilin G acilaze iz providencia rettgeri proizvedene u Pichia pastoris
T1  - Glycosylation and pH stability of penicillin G acylase from providencia rettgeri produced in Pichia pastoris
EP  - 586
IS  - 4
SP  - 581
VL  - 61
DO  - 10.2298/ABS0904581S
ER  - 

@article{
author = "Šenerović, Lidija and Stanković, Nada and Ljubijankić, G. and Vasiljević, Branka",
year = "2009",
abstract = "Penicilin G acilaza (PAC) je jedan od najšire korišćenih enzima u industrijskoj sintezi polusintetskih antibiotika. U ovom radu dobijeni nivo ekspresije PAC gena iz Providencia rettgeri u ekspresionom sistemu Pichia pastoris iznosio je 2.7 U/ml. Rekombinantni enzim je prečišćen i određen je njegov glikozilacioni status. Nađeno je da osim što su obe subjedinice enzima (α i β) N-glikozilovane, β subjedinica sadrži još i O-glikane. Takođe je ustanovljeno da je rekombinantna PACP. rett. stabilna u širokom pH opsegu što ju je, zajedno sa predhodno ustanovljenom visokom termostabilnošću, učinilo izuzetno privlačnim biokatalizatorom sa industrijske tačke gledišta., Penicillin G acylase (PAC) is one of the most widely used enzymes in industrial synthesis of semi-synthetic antibiotics. The Providencia rettgeri pac gene was expressed to a level of 2.7 U/ml using the Pichia pastoris expression system. The recombinant enzyme was purified and its glycosylation status was determined. It was found that both subunits (α and β) of the enzyme were N-glycosylated, while the β-subunit also contained O-glycans. It was also observed that rPACP.rett. was stable in a wide range of pH, which, in addition to the previously proved high thermostability, makes it an attractive biocatalyst from an industrial point of view.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Glikozilacija i pH stabilnost penicilin G acilaze iz providencia rettgeri proizvedene u Pichia pastoris, Glycosylation and pH stability of penicillin G acylase from providencia rettgeri produced in Pichia pastoris",
pages = "586-581",
number = "4",
volume = "61",
doi = "10.2298/ABS0904581S"
}

Šenerović, L., Stanković, N., Ljubijankić, G.,& Vasiljević, B.. (2009). Glikozilacija i pH stabilnost penicilin G acilaze iz providencia rettgeri proizvedene u Pichia pastoris. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 61(4), 581-586.
https://doi.org/10.2298/ABS0904581S

Šenerović L, Stanković N, Ljubijankić G, Vasiljević B. Glikozilacija i pH stabilnost penicilin G acilaze iz providencia rettgeri proizvedene u Pichia pastoris. in Archives of Biological Sciences. 2009;61(4):581-586.
doi:10.2298/ABS0904581S .

Šenerović, Lidija, Stanković, Nada, Ljubijankić, G., Vasiljević, Branka, "Glikozilacija i pH stabilnost penicilin G acilaze iz providencia rettgeri proizvedene u Pichia pastoris" in Archives of Biological Sciences, 61, no. 4 (2009):581-586,
https://doi.org/10.2298/ABS0904581S . .

TY  - JOUR
AU  - Savić, Miloje
AU  - Lovrić, Josip
AU  - Ilić-Tomić, Tatjana
AU  - Vasiljević, Branka
AU  - Conn, Graeme L.
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/375
AB  - The 16S ribosomal RNA methyltransferase enzymes that modify nucleosides in the drug binding site to provide self-resistance in aminoglycoside-producing micro-organisms have been proposed to comprise two distinct groups of S-adenosyl-L-methionine (SAM)-dependent RNA enzymes, namely the Kgm and Kam families. Here, the nucleoside methylation sites for three Kgm family methyltransferases, Sgm from Micromonospora zionensis, GrmA from Micromonospora echinospora and Krm from Frankia sp. Ccl3, were experimentally determined as G1405 by MALDI-ToF mass spectrometry. These results significantly extend the list of securely characterized G1405 modifying enzymes and experimentally validate their grouping into a single enzyme family. Heterologous expression of the KamB methyltransferase from Streptoalloteichus tenebrarius experimentally confirmed the requirement for an additional 60 amino acids on the deduced KamB N-terminus to produce an active methyltransferase acting at A1408, as previously suggested by an in silico analysis. Finally, the modifications at G1405 and A1408, were shown to confer partially overlapping but distinct resistance profiles in Escherichia coli. Collectively, these data provide a more secure and systematic basis for classification of new aminoglycoside resistance methyltransferases from producers and pathogenic bacteria on the basis of their sequences and resistance profiles.
PB  - Oxford Univ Press, Oxford
T2  - Nucleic Acids Research
T1  - Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics
EP  - 5431
IS  - 16
SP  - 5420
VL  - 37
DO  - 10.1093/nar/gkp575
ER  - 

@article{
author = "Savić, Miloje and Lovrić, Josip and Ilić-Tomić, Tatjana and Vasiljević, Branka and Conn, Graeme L.",
year = "2009",
abstract = "The 16S ribosomal RNA methyltransferase enzymes that modify nucleosides in the drug binding site to provide self-resistance in aminoglycoside-producing micro-organisms have been proposed to comprise two distinct groups of S-adenosyl-L-methionine (SAM)-dependent RNA enzymes, namely the Kgm and Kam families. Here, the nucleoside methylation sites for three Kgm family methyltransferases, Sgm from Micromonospora zionensis, GrmA from Micromonospora echinospora and Krm from Frankia sp. Ccl3, were experimentally determined as G1405 by MALDI-ToF mass spectrometry. These results significantly extend the list of securely characterized G1405 modifying enzymes and experimentally validate their grouping into a single enzyme family. Heterologous expression of the KamB methyltransferase from Streptoalloteichus tenebrarius experimentally confirmed the requirement for an additional 60 amino acids on the deduced KamB N-terminus to produce an active methyltransferase acting at A1408, as previously suggested by an in silico analysis. Finally, the modifications at G1405 and A1408, were shown to confer partially overlapping but distinct resistance profiles in Escherichia coli. Collectively, these data provide a more secure and systematic basis for classification of new aminoglycoside resistance methyltransferases from producers and pathogenic bacteria on the basis of their sequences and resistance profiles.",
publisher = "Oxford Univ Press, Oxford",
journal = "Nucleic Acids Research",
title = "Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics",
pages = "5431-5420",
number = "16",
volume = "37",
doi = "10.1093/nar/gkp575"
}

Savić, M., Lovrić, J., Ilić-Tomić, T., Vasiljević, B.,& Conn, G. L.. (2009). Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics. in Nucleic Acids Research
Oxford Univ Press, Oxford., 37(16), 5420-5431.
https://doi.org/10.1093/nar/gkp575

Savić M, Lovrić J, Ilić-Tomić T, Vasiljević B, Conn GL. Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics. in Nucleic Acids Research. 2009;37(16):5420-5431.
doi:10.1093/nar/gkp575 .

Savić, Miloje, Lovrić, Josip, Ilić-Tomić, Tatjana, Vasiljević, Branka, Conn, Graeme L., "Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics" in Nucleic Acids Research, 37, no. 16 (2009):5420-5431,
https://doi.org/10.1093/nar/gkp575 . .

TY  - JOUR
AU  - Savić, Miloje
AU  - Ilić-Tomić, Tatjana
AU  - Macmaster, Rachel
AU  - Vasiljević, Branka
AU  - Conn, Graeme L.
PY  - 2008
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/328
AB  - The 16S rRNA methyltransferase Sgm from "Micromonospora zionensis" confers resistance to aminoglycoside antibiotics by specific modification of the 30S ribosomal A site. Sgm is a member of the FmrO family, distant relatives of the S-adenosyl-L-methionine (SAM)-dependent RNA subfamily of methyltransferase enzymes. Using amino acid conservation across the FmrO family, seven putative key amino acids were selected for mutation to assess their role in forming the SAM cofactor binding pocket or in methyl group transfer. Each mutated residue was found to be essential for Sgm function, as no modified protein could effectively support bacterial growth in liquid media containing gentamicin or methylate 30S subunits in vitro. Using isothermal titration calorimetry, Sgm was found to bind SAM with a K-D (binding constant) of 17.6 mu M, and comparable values were obtained for one functional mutant (N179A) and four proteins modified at amino acids predicted to be involved in catalysis in methyl group transfer. In contrast, none of the G135, D156, or D182 Sgm mutants bound the cofactor, confirming their role in creating the SAM binding pocket. These results represent the first functional characterization of any FmrO methyltransferase and may provide a basis for a further structurefunction analysis of these aminoglycoside resistance determinants.
PB  - Amer Soc Microbiology, Washington
T2  - Journal of Bacteriology
T1  - Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm
EP  - 5861
IS  - 17
SP  - 5855
VL  - 190
DO  - 10.1128/JB.00076-08
ER  - 

@article{
author = "Savić, Miloje and Ilić-Tomić, Tatjana and Macmaster, Rachel and Vasiljević, Branka and Conn, Graeme L.",
year = "2008",
abstract = "The 16S rRNA methyltransferase Sgm from "Micromonospora zionensis" confers resistance to aminoglycoside antibiotics by specific modification of the 30S ribosomal A site. Sgm is a member of the FmrO family, distant relatives of the S-adenosyl-L-methionine (SAM)-dependent RNA subfamily of methyltransferase enzymes. Using amino acid conservation across the FmrO family, seven putative key amino acids were selected for mutation to assess their role in forming the SAM cofactor binding pocket or in methyl group transfer. Each mutated residue was found to be essential for Sgm function, as no modified protein could effectively support bacterial growth in liquid media containing gentamicin or methylate 30S subunits in vitro. Using isothermal titration calorimetry, Sgm was found to bind SAM with a K-D (binding constant) of 17.6 mu M, and comparable values were obtained for one functional mutant (N179A) and four proteins modified at amino acids predicted to be involved in catalysis in methyl group transfer. In contrast, none of the G135, D156, or D182 Sgm mutants bound the cofactor, confirming their role in creating the SAM binding pocket. These results represent the first functional characterization of any FmrO methyltransferase and may provide a basis for a further structurefunction analysis of these aminoglycoside resistance determinants.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Journal of Bacteriology",
title = "Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm",
pages = "5861-5855",
number = "17",
volume = "190",
doi = "10.1128/JB.00076-08"
}

Savić, M., Ilić-Tomić, T., Macmaster, R., Vasiljević, B.,& Conn, G. L.. (2008). Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm. in Journal of Bacteriology
Amer Soc Microbiology, Washington., 190(17), 5855-5861.
https://doi.org/10.1128/JB.00076-08

Savić M, Ilić-Tomić T, Macmaster R, Vasiljević B, Conn GL. Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm. in Journal of Bacteriology. 2008;190(17):5855-5861.
doi:10.1128/JB.00076-08 .

Savić, Miloje, Ilić-Tomić, Tatjana, Macmaster, Rachel, Vasiljević, Branka, Conn, Graeme L., "Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm" in Journal of Bacteriology, 190, no. 17 (2008):5855-5861,
https://doi.org/10.1128/JB.00076-08 . .

TY  - JOUR
AU  - Ilić-Tomić, Tatjana
AU  - Morić, Ivana
AU  - Conn, Graeme L.
AU  - Vasiljević, Branka
PY  - 2008
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/324
AB  - The aminoglycoside resistance genes sgm from Micromonospora zionensis and kgmB from Streptomyces tenebrarius were cloned into a yeast expression vector to test whether the encoded prokaryotic methylases can modify the 18S rRNA A-site and thus confer resistance to G-418. Despite the detectable presence of mRNAs in yeast cells, neither G-418-resistant yeast transformants nor positive western blot signals were obtained. Neither methylase was capable of methylating 40S subunits despite very high conservation of the antibiotic rRNA binding sites. However, the results provide novel insight into the action of Sgm by showing that it methylates the same site as KgmB, i.e. G1405 in 16S rRNA.
PB  - Elsevier Science Bv, Amsterdam
T2  - Research in Microbiology
T1  - Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site
EP  - 662
IS  - 9-10
SP  - 658
VL  - 159
DO  - 10.1016/j.resmic.2008.09.006
ER  - 

@article{
author = "Ilić-Tomić, Tatjana and Morić, Ivana and Conn, Graeme L. and Vasiljević, Branka",
year = "2008",
abstract = "The aminoglycoside resistance genes sgm from Micromonospora zionensis and kgmB from Streptomyces tenebrarius were cloned into a yeast expression vector to test whether the encoded prokaryotic methylases can modify the 18S rRNA A-site and thus confer resistance to G-418. Despite the detectable presence of mRNAs in yeast cells, neither G-418-resistant yeast transformants nor positive western blot signals were obtained. Neither methylase was capable of methylating 40S subunits despite very high conservation of the antibiotic rRNA binding sites. However, the results provide novel insight into the action of Sgm by showing that it methylates the same site as KgmB, i.e. G1405 in 16S rRNA.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Research in Microbiology",
title = "Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site",
pages = "662-658",
number = "9-10",
volume = "159",
doi = "10.1016/j.resmic.2008.09.006"
}

Ilić-Tomić, T., Morić, I., Conn, G. L.,& Vasiljević, B.. (2008). Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site. in Research in Microbiology
Elsevier Science Bv, Amsterdam., 159(9-10), 658-662.
https://doi.org/10.1016/j.resmic.2008.09.006

Ilić-Tomić T, Morić I, Conn GL, Vasiljević B. Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site. in Research in Microbiology. 2008;159(9-10):658-662.
doi:10.1016/j.resmic.2008.09.006 .

Ilić-Tomić, Tatjana, Morić, Ivana, Conn, Graeme L., Vasiljević, Branka, "Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site" in Research in Microbiology, 159, no. 9-10 (2008):658-662,
https://doi.org/10.1016/j.resmic.2008.09.006 . .

TY  - JOUR
AU  - Kojić, Milan
AU  - Vojnović, Sandra
AU  - Vukov, Nataša
AU  - Vasiljević, Branka
PY  - 2007
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/287
AB  - 16S rRNK metilaze su eksprimirane u većini bakterija koje proizvode antibiotike da bi se zaštitile od dejstva antibiotika putem metilacije 16S rRNK na pozicijama koje su bitne za njihovo dejstvo. Gen sgm koji je odgovoran za rezistenciju na sisomicin i gentamicin u soju Micromonospora zionensis, metilu je G1405 u okviru A mesta 16S rRNA gde se nalazi i CCGCCC heksanukleotid. Isti heksanukleotid se nalazi i 14 nukleotida ispred mesta vezivanja ribozoma na sgm informacionoj RNK. Predloženi model translacione regulacije sgm gena pretpostavlja da se Sgm protein vezuje za ovaj motiv kako na 16S rRNK, tako i na 5’ netranslirajućem regionu (UTR) sopstvene informacione RNK. 5’ UTR sekvenca je overeksprimirana na sgm informacionoj RNK sa skraćenim 3’ krajem i testiran je efekat na gentamicinsku rezistenciju u ćelijama E. coli i Micromonospora melanosporea. Overekspresija ove regulatorne sekvence dovodi do smanjenja rezistencije u oba testirana soja najverovatnije zbog titracije Sgm molekula od strane 5’ UTR-a.
AB  - The 16S rRNA methylases are expressed by most of the antibiotic producing bacteria in order to protect themselves against antibiotics by methylation of 16S rRNA at positions which are crucial for their action. The sgm sisomicin-gentamicin resistance gene from Micromonospora zionensis methylates G1405 positioned in the A site of 16S rRNA, which includes a CCGCCC hexanucleotide. The same hexanucleotide is also present 14 nucleotides in front of the ribosome binding site of sgm mRNA. The model proposed for translational regulation of sgm assumes that Sgm binds to this motif, both on 16S rRNA and on the 5’ untranslated region (UTR) of its own mRNA. The 5’ UTR mRNA sequence was overexpressed on 3’-truncated sgm mRNA, and the effect on gentamicin resistance conferred by Sgm was tested in Escherichia coli and in Micromonospora melanosporea. Overexpression of the sgm mRNA regulatory region decreases the resistance to gentamicin in both E. coli and M. melanosporea. This effect is likely to be due to titration of Sgm molecules by the overexpressed 5’ UTR.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Overekspresija 5’ UTR mRNK sgm gena smanjuje rezistenciju na gentamicin u ćelijama Escherichia coli i Micromonospora melanosporea
T1  - Overexpression of sgm 5’ UTR mRNA reduces gentamicin resistance in both Escherichia coli and Micromonospora melanosporea cells
EP  - 280
IS  - 4
SP  - 273
VL  - 59
DO  - 10.2298/ABS0704273K
ER  - 

@article{
author = "Kojić, Milan and Vojnović, Sandra and Vukov, Nataša and Vasiljević, Branka",
year = "2007",
abstract = "16S rRNK metilaze su eksprimirane u većini bakterija koje proizvode antibiotike da bi se zaštitile od dejstva antibiotika putem metilacije 16S rRNK na pozicijama koje su bitne za njihovo dejstvo. Gen sgm koji je odgovoran za rezistenciju na sisomicin i gentamicin u soju Micromonospora zionensis, metilu je G1405 u okviru A mesta 16S rRNA gde se nalazi i CCGCCC heksanukleotid. Isti heksanukleotid se nalazi i 14 nukleotida ispred mesta vezivanja ribozoma na sgm informacionoj RNK. Predloženi model translacione regulacije sgm gena pretpostavlja da se Sgm protein vezuje za ovaj motiv kako na 16S rRNK, tako i na 5’ netranslirajućem regionu (UTR) sopstvene informacione RNK. 5’ UTR sekvenca je overeksprimirana na sgm informacionoj RNK sa skraćenim 3’ krajem i testiran je efekat na gentamicinsku rezistenciju u ćelijama E. coli i Micromonospora melanosporea. Overekspresija ove regulatorne sekvence dovodi do smanjenja rezistencije u oba testirana soja najverovatnije zbog titracije Sgm molekula od strane 5’ UTR-a., The 16S rRNA methylases are expressed by most of the antibiotic producing bacteria in order to protect themselves against antibiotics by methylation of 16S rRNA at positions which are crucial for their action. The sgm sisomicin-gentamicin resistance gene from Micromonospora zionensis methylates G1405 positioned in the A site of 16S rRNA, which includes a CCGCCC hexanucleotide. The same hexanucleotide is also present 14 nucleotides in front of the ribosome binding site of sgm mRNA. The model proposed for translational regulation of sgm assumes that Sgm binds to this motif, both on 16S rRNA and on the 5’ untranslated region (UTR) of its own mRNA. The 5’ UTR mRNA sequence was overexpressed on 3’-truncated sgm mRNA, and the effect on gentamicin resistance conferred by Sgm was tested in Escherichia coli and in Micromonospora melanosporea. Overexpression of the sgm mRNA regulatory region decreases the resistance to gentamicin in both E. coli and M. melanosporea. This effect is likely to be due to titration of Sgm molecules by the overexpressed 5’ UTR.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Overekspresija 5’ UTR mRNK sgm gena smanjuje rezistenciju na gentamicin u ćelijama Escherichia coli i Micromonospora melanosporea, Overexpression of sgm 5’ UTR mRNA reduces gentamicin resistance in both Escherichia coli and Micromonospora melanosporea cells",
pages = "280-273",
number = "4",
volume = "59",
doi = "10.2298/ABS0704273K"
}

Kojić, M., Vojnović, S., Vukov, N.,& Vasiljević, B.. (2007). Overekspresija 5’ UTR mRNK sgm gena smanjuje rezistenciju na gentamicin u ćelijama Escherichia coli i Micromonospora melanosporea. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 59(4), 273-280.
https://doi.org/10.2298/ABS0704273K

Kojić M, Vojnović S, Vukov N, Vasiljević B. Overekspresija 5’ UTR mRNK sgm gena smanjuje rezistenciju na gentamicin u ćelijama Escherichia coli i Micromonospora melanosporea. in Archives of Biological Sciences. 2007;59(4):273-280.
doi:10.2298/ABS0704273K .

Kojić, Milan, Vojnović, Sandra, Vukov, Nataša, Vasiljević, Branka, "Overekspresija 5’ UTR mRNK sgm gena smanjuje rezistenciju na gentamicin u ćelijama Escherichia coli i Micromonospora melanosporea" in Archives of Biological Sciences, 59, no. 4 (2007):273-280,
https://doi.org/10.2298/ABS0704273K . .