Inducible expression of choline sulfatase and its regulator BetR in Pseudomonas sp ATCC19151
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2011
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Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
Transcriptional regulation of gene expression / Pseudomonas / Osmoprotection / Choline sulfataseIzvor:
Archives of Microbiology, 2011, 193, 6, 399-405Izdavač:
- Springer, New York
Finansiranje / projekti:
- Izučavanje regulacije ekspresije gena odabranih industrijskih mikroorganizama (RS-MESTD-MPN2006-2010-143036)
DOI: 10.1007/s00203-011-0685-x
ISSN: 0302-8933
PubMed: 21369825
WoS: 000290725900002
Scopus: 2-s2.0-79958230693
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .