Transcriptional activation of quinoline degradation operons of Pseudomonas putida 86 by the AraC/XylS-type regulator OxoS and cross-regulation of the PqorM promoter by XylS.

@article{citeulike:3037585, abstract = {The quinoline-degradative gene cluster (oxoO, open reading frames 1 to 6 [ORF1 to -6], qorMSL, ORF7 to -9, oxoR) of Pseudomonas putida 86 consists of several overlapping operons controlled in response to quinoline by the master promoter PoxoO and internal promoters Porf3, PqorM, and PoxoR. ORF7 to -9, presumed to be important for maturation of the molybdenum hydroxylase quinoline 2-oxidoreductase, are also weakly transcribed independently of quinoline. Expression of the oxoS gene, located upstream of oxoO, is not influenced by the carbon source. OxoS shows 26\% amino acid sequence identity to XylS, the transcriptional regulator of the meta pathway promoter Pm of TOL plasmid pWW0, and is required for quinoline-dependent transcription from PoxoO, Porf3, PqorM, and PoxoR. 5' deletion analysis of PoxoO and PqorM suggested that a 5'-TGCPuCT-N3-GGGATA-3' motif, which resembles the distal 5'-TGCA-N6-GGNTA-3' half-site of the tandem XylS binding site, is essential for oxoS-dependent transcriptional activation. PqorM, which shows similarity to the tandem XylS recognition site of Pm, was cross-activated by the xylS gene product in response to benzoate. The distal half-site of PqorM is necessary, but probably not sufficient, for transcriptional activation by XylS. Despite conservation in PoxoO of a distal 5'-TGCA-N6-GGNTA-3' sequence, cross-activation of PoxoO by XylS and benzoate was not observed. The oxoS gene product in the presence of quinoline weakly stimulated transcription from the Pm promoter. Involvement of an XylS-type protein in the regulation of genes encoding synthesis of a molybdenum hydroxylase is without precedent and may reflect the evolutionary origin of this pathway in the metabolism of aromatic compounds.}, address = {Institut f\"{u}r Molekulare Mikrobiologie und Biotechnologie, Westf\"{a}lische Wilhelms-Universit\"{a}t M\"{u}nster, Corrensstrasse 3, D-48149 M\"{u}nster, Germany.}, author = {Carl, B. and Fetzner, S. }, citeulike-article-id = {3037585}, doi = {10.1128/AEM.71.12.8618-8626.2005}, issn = {0099-2240}, journal = {Applied and environmental microbiology}, keywords = {biodegradation, for-the-review, quinoline, regulation, transcription, xyls}, month = {December}, number = {12}, pages = {8618--8626}, posted-at = {2008-07-23 20:13:17}, priority = {3}, title = {Transcriptional activation of quinoline degradation operons of Pseudomonas putida 86 by the AraC/XylS-type regulator OxoS and cross-regulation of the PqorM promoter by XylS.}, url = {http://dx.doi.org/10.1128/AEM.71.12.8618-8626.2005}, volume = {71}, year = {2005} }

TY - JOUR ID - citeulike:3037585 L3 - citeulike-article-id:3037585 TI - Transcriptional activation of quinoline degradation operons of Pseudomonas putida 86 by the AraC/XylS-type regulator OxoS and cross-regulation of the PqorM promoter by XylS. JF - Applied and environmental microbiology VL - 71 IS - 12 SP - 8618 EP - 8626 AD - Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, D-48149 Münster, Germany. SN - 0099-2240 N2 - The quinoline-degradative gene cluster (oxoO, open reading frames 1 to 6 [ORF1 to -6], qorMSL, ORF7 to -9, oxoR) of Pseudomonas putida 86 consists of several overlapping operons controlled in response to quinoline by the master promoter PoxoO and internal promoters Porf3, PqorM, and PoxoR. ORF7 to -9, presumed to be important for maturation of the molybdenum hydroxylase quinoline 2-oxidoreductase, are also weakly transcribed independently of quinoline. Expression of the oxoS gene, located upstream of oxoO, is not influenced by the carbon source. OxoS shows 26% amino acid sequence identity to XylS, the transcriptional regulator of the meta pathway promoter Pm of TOL plasmid pWW0, and is required for quinoline-dependent transcription from PoxoO, Porf3, PqorM, and PoxoR. 5' deletion analysis of PoxoO and PqorM suggested that a 5'-TGCPuCT-N3-GGGATA-3' motif, which resembles the distal 5'-TGCA-N6-GGNTA-3' half-site of the tandem XylS binding site, is essential for oxoS-dependent transcriptional activation. PqorM, which shows similarity to the tandem XylS recognition site of Pm, was cross-activated by the xylS gene product in response to benzoate. The distal half-site of PqorM is necessary, but probably not sufficient, for transcriptional activation by XylS. Despite conservation in PoxoO of a distal 5'-TGCA-N6-GGNTA-3' sequence, cross-activation of PoxoO by XylS and benzoate was not observed. The oxoS gene product in the presence of quinoline weakly stimulated transcription from the Pm promoter. Involvement of an XylS-type protein in the regulation of genes encoding synthesis of a molybdenum hydroxylase is without precedent and may reflect the evolutionary origin of this pathway in the metabolism of aromatic compounds. KW - biodegradation KW - for-the-review KW - quinoline KW - regulation KW - transcription KW - xyls AU - Carl, B AU - Fetzner, S PY - 2005/12// UR - http://dx.doi.org/10.1128/AEM.71.12.8618-8626.2005 ER -