Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-1-11
pubmed:databankReference
pubmed:abstractText
In Pseudomonas aeruginosa PAO1, expression of elastase is dependent upon an interaction between the positive transcriptional activator LasR and the auto-inducer molecule N-(3-oxododecanoyl)-L-homoserine lactone (OdDHL), the synthesis of which is directed by LasI. Previously we have shown that in PAN067, an elastase-negative mutant of PAO1, elastase production can be restored to some extent by addition of exogenous N-(3-oxohexanoyl)-L-homoserine lactone (OHHL). Here we report that PAN067 is also defective in the production of alkaline protease, haemolysin, cyanide, pyocyanin and autoinducer(s). As neither addition of exogenous OdDHL nor introduction of lasR restored PAN067 to the parental phenotype, we sought to complement PAN067 with PAO1 DNA. From a cosmid library, a 2 kb DNA fragment was identified which re-established production of autoinducer(s) and exoproducts in PAN067. From the nucleotide sequence of this fragment, two genes termed rhIR and rhII were identified. RhII is responsible for autoinducer synthesis and shares 31% homology with LasI; RhIR has been previously identified in P. aeruginosa strain DSM2659 as a regulator of rhamnolipid biosynthesis and shares 28% identity with LasR. These data provide clear evidence that multiple families of quorum-sensing modulons interactively regulate gene expression in P. aeruginosa.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Homoserine, http://linkedlifedata.com/resource/pubmed/chemical/Lactones, http://linkedlifedata.com/resource/pubmed/chemical/LasI protein, Pseudomonas aeruginosa, http://linkedlifedata.com/resource/pubmed/chemical/LasR protein, Pseudomonas aeruginosa, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/LuxI protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/LuxR autoinducer binding proteins, http://linkedlifedata.com/resource/pubmed/chemical/Pseudomonas aeruginosa autoinducer, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/rhiR protein, Rhizobium...
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
333-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7494482-Amino Acid Sequence, pubmed-meshheading:7494482-Bacterial Proteins, pubmed-meshheading:7494482-Base Sequence, pubmed-meshheading:7494482-Cloning, Molecular, pubmed-meshheading:7494482-DNA-Binding Proteins, pubmed-meshheading:7494482-Gene Expression Regulation, Bacterial, pubmed-meshheading:7494482-Genetic Complementation Test, pubmed-meshheading:7494482-Homoserine, pubmed-meshheading:7494482-Lactones, pubmed-meshheading:7494482-Ligases, pubmed-meshheading:7494482-Molecular Sequence Data, pubmed-meshheading:7494482-Pseudomonas aeruginosa, pubmed-meshheading:7494482-Repressor Proteins, pubmed-meshheading:7494482-Sequence Analysis, DNA, pubmed-meshheading:7494482-Sequence Homology, Amino Acid, pubmed-meshheading:7494482-Trans-Activators, pubmed-meshheading:7494482-Transcription Factors, pubmed-meshheading:7494482-Virulence
pubmed:year
1995
pubmed:articleTitle
Multiple homologues of LuxR and LuxI control expression of virulence determinants and secondary metabolites through quorum sensing in Pseudomonas aeruginosa PAO1.
pubmed:affiliation
Laboratoire d'Ingenierie et Dynamique des Systémes Membranaires, Centre National de la Recherche Scientifique, Marseille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't