Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358
Апстракт
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 occurr...ed 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.
Кључне речи:
protocatechuic acid / pobC / pobA / aromatic acidИзвор:
Microbiology-Sgm, 2001, 147, 1611-1620Издавач:
- Soc General Microbiology, Reading
DOI: 10.1099/00221287-147-6-1611
ISSN: 1350-0872
PubMed: 11390692
WoS: 000169194100024
Scopus: 2-s2.0-0034977060
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Bertani, I AU - Kojić, Milan AU - Venturi, V PY - 2001 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/158 AB - The regulation of the p-hydroxybenzoate hydroxylase gene (pobA) of Pseudomonas putida WC5358 involved in the catabolism of p-hydroxybenzoic acid (PHB) to the central intermediate protocatechuate was studied. Protocatechuic acid (PCA) is then degraded via the beta -ketoadipate pathway to form tricarboxylic acid intermediates. In several Gram-negative bacteria pobA has been found genetically linked to a regulator called pobR which activates pobA expression in response to PHB, In this study the identification and characterization of the pobC-pobA locus of P, putida WCS358 is presented. The p-hydroxybenzoate hydroxylase (PobA) is highly identical to other identified PobA proteins, whereas the regulatory protein PobC did not display very high identity to other PobR proteins studied and belonged to the AraC family of regulatory proteins, hence it has been designated PobC, Using the pobA promoter transcriptionally fused to a promoterless lad gene it was observed that induction via PobC occurred very efficiently when PHB was present and to a lesser but still significant level also in the presence of PCA, This PobC-PCA response was genetically demonstrated by making use of pobC::Tn5 and pcaH::Tn5 mutants of strain WC5358 constructed in this study. In pobC mutants both the p-hydroxybenzoic and PCA response were not observed, whereas in the pcaH mutant, which lacks a functional protocatechuate 3,4-dioxygenase, the protocatechuic-acid-dependent pobA activation was still observed. Finally, the activation of pobA by PHB varied according to the concentration and it was observed that in the pcaR::Tn5 regulatory mutant of strain WCS358 the pobA promoter activity was reduced. PcaR is a regulator involved in the regulation of several loci of the beta -ketoadipate pathway, one of which is pcaK, It was postulated that the reduction of pobA activation in pcaR::Tn5 mutants was because there was no expression of the pcaK gene encoding the PHB transport protein resulting in lower levels of PHB present inside the cell. PB - Soc General Microbiology, Reading T2 - Microbiology-Sgm T1 - Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358 EP - 1620 SP - 1611 VL - 147 DO - 10.1099/00221287-147-6-1611 ER -
@article{ author = "Bertani, I and Kojić, Milan and Venturi, V", year = "2001", abstract = "The regulation of the p-hydroxybenzoate hydroxylase gene (pobA) of Pseudomonas putida WC5358 involved in the catabolism of p-hydroxybenzoic acid (PHB) to the central intermediate protocatechuate was studied. Protocatechuic acid (PCA) is then degraded via the beta -ketoadipate pathway to form tricarboxylic acid intermediates. In several Gram-negative bacteria pobA has been found genetically linked to a regulator called pobR which activates pobA expression in response to PHB, In this study the identification and characterization of the pobC-pobA locus of P, putida WCS358 is presented. The p-hydroxybenzoate hydroxylase (PobA) is highly identical to other identified PobA proteins, whereas the regulatory protein PobC did not display very high identity to other PobR proteins studied and belonged to the AraC family of regulatory proteins, hence it has been designated PobC, Using the pobA promoter transcriptionally fused to a promoterless lad gene it was observed that induction via PobC occurred very efficiently when PHB was present and to a lesser but still significant level also in the presence of PCA, This PobC-PCA response was genetically demonstrated by making use of pobC::Tn5 and pcaH::Tn5 mutants of strain WC5358 constructed in this study. In pobC mutants both the p-hydroxybenzoic and PCA response were not observed, whereas in the pcaH mutant, which lacks a functional protocatechuate 3,4-dioxygenase, the protocatechuic-acid-dependent pobA activation was still observed. Finally, the activation of pobA by PHB varied according to the concentration and it was observed that in the pcaR::Tn5 regulatory mutant of strain WCS358 the pobA promoter activity was reduced. PcaR is a regulator involved in the regulation of several loci of the beta -ketoadipate pathway, one of which is pcaK, It was postulated that the reduction of pobA activation in pcaR::Tn5 mutants was because there was no expression of the pcaK gene encoding the PHB transport protein resulting in lower levels of PHB present inside the cell.", publisher = "Soc General Microbiology, Reading", journal = "Microbiology-Sgm", title = "Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358", pages = "1620-1611", volume = "147", doi = "10.1099/00221287-147-6-1611" }
Bertani, I., Kojić, M.,& Venturi, V.. (2001). Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358. in Microbiology-Sgm Soc General Microbiology, Reading., 147, 1611-1620. https://doi.org/10.1099/00221287-147-6-1611
Bertani I, Kojić M, Venturi V. Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358. in Microbiology-Sgm. 2001;147:1611-1620. doi:10.1099/00221287-147-6-1611 .
Bertani, I, Kojić, Milan, Venturi, V, "Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358" in Microbiology-Sgm, 147 (2001):1611-1620, https://doi.org/10.1099/00221287-147-6-1611 . .