Venturi, V

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  • Venturi, V (8)
  • Venturi, V. (1)
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Author's Bibliography

Regulation of the sdsA alkyl sulfatase of Pseudomonas sp ATCC19151 and its involvement in degradation of anionic surfactants

Jovčić, Branko; Venturi, V.; Davison, J.; Topisirović, Ljubiša; Kojić, Milan

(Wiley-Blackwell, Malden, 2010)

TY  - JOUR
AU  - Jovčić, Branko
AU  - Venturi, V.
AU  - Davison, J.
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/822
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 . .
23
16
22

Novel target genes of PsrA transcriptional regulator of Pseudomonas aeruginosa

Kojić, Milan; Jovčić, Branko; Vindigni, A; Odreman, F; Venturi, V

(Wiley-Blackwell, Hoboken, 2005)

TY  - JOUR
AU  - Kojić, Milan
AU  - Jovčić, Branko
AU  - Vindigni, A
AU  - Odreman, F
AU  - Venturi, V
PY  - 2005
UR  - http://intor.torlakinstitut.com/handle/123456789/802
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 . .
30
23
29

Role of GacA, LasI, RhlI, ppk, PsrA, vfr and ClpXP in the regulation of the stationary-phase sigma factor rpoS/RpoS in Pseudomonas

Bertani, I; Sevo, M; Kojić, Milan; Venturi, V

(Springer-Verlag, New York, 2003)

TY  - JOUR
AU  - Bertani, I
AU  - Sevo, M
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2003
UR  - http://intor.torlakinstitut.com/handle/123456789/799
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 . .
3
38
37

Identification of quorum-sensing-regulated genes of Burkholderia cepacia

Aguilar, C; Friscina, A; Devescovi, G; Kojić, Milan; Venturi, V

(Amer Soc Microbiology, Washington, 2003)

TY  - JOUR
AU  - Aguilar, C
AU  - Friscina, A
AU  - Devescovi, G
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2003
UR  - http://intor.torlakinstitut.com/handle/123456789/798
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 . .
40
41

TetR family member PsrA directly binds the Pseudomonas rpoS and psrA promoters

Kojić, Milan; Aguilar, C; Venturi, V

(Amer Soc Microbiology, Washington, 2002)

TY  - JOUR
AU  - Kojić, Milan
AU  - Aguilar, C
AU  - Venturi, V
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/797
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 . .
53
50

Regulation of rpoS gene expression in Pseudomonas: involvement of a TetR family regulator

Kojić, Milan; Venturi, V

(Amer Soc Microbiology, Washington, 2001)

TY  - JOUR
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2001
UR  - http://intor.torlakinstitut.com/handle/123456789/795
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 . .
74
73

Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358

Bertani, I; Kojić, Milan; Venturi, V

(Soc General Microbiology, Reading, 2001)

TY  - JOUR
AU  - Bertani, I
AU  - Kojić, Milan
AU  - Venturi, V
PY  - 2001
UR  - http://intor.torlakinstitut.com/handle/123456789/794
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 . .
39
38

The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity

Degrassi, G; Kojić, Milan; Ljubijankić, G; Venturi, V

(Microbiology Soc, London, 2000)

TY  - JOUR
AU  - Degrassi, G
AU  - Kojić, Milan
AU  - Ljubijankić, G
AU  - Venturi, V
PY  - 2000
UR  - http://intor.torlakinstitut.com/handle/123456789/791
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 . .
3
50
51

Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production

Kojić, Milan; Degrassi, G; Venturi, V

(Elsevier, Amsterdam, 1999)

TY  - JOUR
AU  - Kojić, Milan
AU  - Degrassi, G
AU  - Venturi, V
PY  - 1999
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/127
UR  - http://intor.torlakinstitut.com/handle/123456789/722
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 . .
34
32