pubmed-article:18547423 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18547423 | lifeskim:mentions | umls-concept:C0033811 | lld:lifeskim |
pubmed-article:18547423 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:18547423 | lifeskim:mentions | umls-concept:C1154823 | lld:lifeskim |
pubmed-article:18547423 | lifeskim:mentions | umls-concept:C1158773 | lld:lifeskim |
pubmed-article:18547423 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:18547423 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:18547423 | pubmed:dateCreated | 2008-7-1 | lld:pubmed |
pubmed-article:18547423 | pubmed:abstractText | In Pseudomonas fluorescens ST, the promoter of the styrene catabolic operon, PstyA, is induced by styrene and is subject to catabolite repression. PstyA regulation relies on the StyS/StyR two-component system and on the IHF global regulator. The phosphorylated response regulator StyR (StyR-P) activates PstyA in inducing conditions when it binds to the high-affinity site STY2, located about -40 bp from the transcription start point. A cis-acting element upstream of STY2, named URE, contains a low-affinity StyR-P binding site (STY1), overlapping the IHF binding site. Deletion of the URE led to a decrease of promoter activity in inducing conditions and to a partial release of catabolite repression. This study was undertaken to assess the relative role played by IHF and StyR-P on the URE, and to clarify if PstyA catabolite repression could rely on the interplay of these regulators. | lld:pubmed |
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pubmed-article:18547423 | pubmed:language | eng | lld:pubmed |
pubmed-article:18547423 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18547423 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18547423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18547423 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18547423 | pubmed:issn | 1471-2180 | lld:pubmed |
pubmed-article:18547423 | pubmed:author | pubmed-author:ZennaroElisab... | lld:pubmed |
pubmed-article:18547423 | pubmed:author | pubmed-author:LeoniLiviaL | lld:pubmed |
pubmed-article:18547423 | pubmed:author | pubmed-author:RampioniGiord... | lld:pubmed |
pubmed-article:18547423 | pubmed:author | pubmed-author:PietrangeliBi... | lld:pubmed |
pubmed-article:18547423 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18547423 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:18547423 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18547423 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18547423 | pubmed:pagination | 92 | lld:pubmed |
pubmed-article:18547423 | pubmed:dateRevised | 2010-9-22 | lld:pubmed |
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pubmed-article:18547423 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18547423 | pubmed:articleTitle | The interplay of StyR and IHF regulates substrate-dependent induction and carbon catabolite repression of styrene catabolism genes in Pseudomonas fluorescens ST. | lld:pubmed |
pubmed-article:18547423 | pubmed:affiliation | Department of Biology, University Roma Tre, Viale Marconi 446, 00146, Rome, Italy. rampioni@uniroma3.it | lld:pubmed |
pubmed-article:18547423 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18547423 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18547423 | lld:entrezgene |
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