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dc.contributor.authorFraley, Cresson D.
dc.contributor.authorRashid, M. Harunur
dc.contributor.authorLee, Sam S. K.
dc.contributor.authorGottschalk, Rebecca
dc.contributor.authorHarrison, Janine
dc.contributor.authorWood, Pauline J.
dc.contributor.authorBrown, Michael R. W.
dc.contributor.authorKornberg, Arthur
dc.date.accessioned2008-05-22T14:55:47Z
dc.date.available2008-05-22T14:55:47Z
dc.date.issued2007
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 104 (9): 3526-3531
dc.identifier.issn0027-8424
dc.identifier.pmid17360677
dc.identifier.doi10.1073/pnas.0609733104
dc.identifier.urihttp://hdl.handle.net/2436/27672
dc.description.abstractPseudomonas aeruginosa, of medical, environmental, and industrial importance, depends on inorganic polyphosphate (poly P) for a wide range of functions, especially survival. Mutants of PAO1 lacking poly P kinase 1, PPK1, the enzyme responsible for most poly P synthesis in Escherichia coli and other bacteria, are defective in motility, quorum sensing, biofilm formation, and virulence. We describe here multiple defects in the ppk1 mutant PAOM5, including a striking compaction of the nucleoid, distortion of the cell envelope, lack of planktonic motility and exopolymer production, and susceptibility to the beta-lactam antibiotic carbenicillin as well as desiccation. We propose that P. aeruginosa with reduced poly P levels undergoes ultrastructural changes that contribute to profound deficiencies in cellular functions.
dc.language.isoen
dc.publisherNational Academy of Sciences
dc.relation.urlhttp://www.pnas.org/cgi/content/full/104/9/3526
dc.subjectCarbenicillin
dc.subjectExopolymer
dc.subjectMotility
dc.subjectDesiccation
dc.subjectNucleoid
dc.subject.meshCarbenicillin
dc.subject.meshCell Membrane
dc.subject.meshChromatography, Thin Layer
dc.subject.meshMicroscopy, Electron
dc.subject.meshMutagenesis
dc.subject.meshMutation
dc.subject.meshPhosphotransferases (Phosphate Group Acceptor)
dc.subject.meshPseudomonas aeruginosa
dc.titleA polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects.
dc.typeJournal article
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of America
html.description.abstractPseudomonas aeruginosa, of medical, environmental, and industrial importance, depends on inorganic polyphosphate (poly P) for a wide range of functions, especially survival. Mutants of PAO1 lacking poly P kinase 1, PPK1, the enzyme responsible for most poly P synthesis in Escherichia coli and other bacteria, are defective in motility, quorum sensing, biofilm formation, and virulence. We describe here multiple defects in the ppk1 mutant PAOM5, including a striking compaction of the nucleoid, distortion of the cell envelope, lack of planktonic motility and exopolymer production, and susceptibility to the beta-lactam antibiotic carbenicillin as well as desiccation. We propose that P. aeruginosa with reduced poly P levels undergoes ultrastructural changes that contribute to profound deficiencies in cellular functions.


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