A polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects.

2.50
Hdl Handle:
http://hdl.handle.net/2436/27672
Title:
A polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects.
Authors:
Fraley, Cresson D.; Rashid, M. Harunur; Lee, Sam S. K.; Gottschalk, Rebecca; Harrison, Janine; Wood, Pauline J.; Brown, Michael R. W.; Kornberg, Arthur
Abstract:
Pseudomonas 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.
Citation:
Proceedings of the National Academy of Sciences of the United States of America, 104 (9): 3526-3531
Publisher:
National Academy of Sciences
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Issue Date:
2007
URI:
http://hdl.handle.net/2436/27672
DOI:
10.1073/pnas.0609733104
PubMed ID:
17360677
Additional Links:
http://www.pnas.org/cgi/content/full/104/9/3526
Type:
Article
Language:
en
ISSN:
0027-8424
Appears in Collections:
Molecular Pharmacology Research Group

Full metadata record

DC FieldValue Language
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): 3526-3531en
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.en
dc.language.isoenen
dc.publisherNational Academy of Sciencesen
dc.relation.urlhttp://www.pnas.org/cgi/content/full/104/9/3526en
dc.subjectCarbenicillinen
dc.subjectExopolymeren
dc.subjectMotilityen
dc.subjectDesiccationen
dc.subjectNucleoiden
dc.subject.meshCarbenicillinen
dc.subject.meshCell Membraneen
dc.subject.meshChromatography, Thin Layeren
dc.subject.meshMicroscopy, Electronen
dc.subject.meshMutagenesisen
dc.subject.meshMutationen
dc.subject.meshPhosphotransferases (Phosphate Group Acceptor)en
dc.subject.meshPseudomonas aeruginosaen
dc.titleA polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects.en
dc.typeArticleen
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaen

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