Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2004-7-2
pubmed:abstractText
Denitrification and arginine fermentation are central metabolic processes performed by the opportunistic pathogen Pseudomonas aeruginosa during biofilm formation and infection of lungs of patients with cystic fibrosis. Genome-wide searches for additional components of the anaerobic metabolism identified potential genes for pyruvate-metabolizing NADH-dependent lactate dehydrogenase (ldhA), phosphotransacetylase (pta), and acetate kinase (ackA). While pyruvate fermentation alone does not sustain significant anaerobic growth of P. aeruginosa, it provides the bacterium with the metabolic capacity for long-term survival of up to 18 days. Detected conversion of pyruvate to lactate and acetate is dependent on the presence of intact ldhA and ackA-pta loci, respectively. DNA microarray studies in combination with reporter gene fusion analysis and enzyme activity measurements demonstrated the anr- and ihfA-dependent anaerobic induction of the ackA-pta promoter. Potential Anr and integration host factor binding sites were localized. Pyruvate-dependent anaerobic long-term survival was found to be significantly reduced in anr and ihfA mutants. No obvious ldhA regulation by oxygen tension was observed. Pyruvate fermentation is pH dependent. Nitrate respiration abolished pyruvate fermentation, while arginine fermentation occurs independently of pyruvate utilization.
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ANR protein, Pseudomonas aeruginosa, http://linkedlifedata.com/resource/pubmed/chemical/Acetate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Acetates, http://linkedlifedata.com/resource/pubmed/chemical/Arginine, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Integration Host Factors, http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Lactic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Nitrates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphate Acetyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9193
pubmed:author
pubmed:copyrightInfo
Copyright 2004 American Society for Microbiology
pubmed:issnType
Print
pubmed:volume
186
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4596-604
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
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