A polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects.
dc.contributor.author | Fraley, Cresson D. | |
dc.contributor.author | Rashid, M. Harunur | |
dc.contributor.author | Lee, Sam S. K. | |
dc.contributor.author | Gottschalk, Rebecca | |
dc.contributor.author | Harrison, Janine | |
dc.contributor.author | Wood, Pauline J. | |
dc.contributor.author | Brown, Michael R. W. | |
dc.contributor.author | Kornberg, Arthur | |
dc.date.accessioned | 2008-05-22T14:55:47Z | |
dc.date.available | 2008-05-22T14:55:47Z | |
dc.date.issued | 2007 | |
dc.identifier.citation | Proceedings of the National Academy of Sciences of the United States of America, 104 (9): 3526-3531 | |
dc.identifier.issn | 0027-8424 | |
dc.identifier.pmid | 17360677 | |
dc.identifier.doi | 10.1073/pnas.0609733104 | |
dc.identifier.uri | http://hdl.handle.net/2436/27672 | |
dc.description.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. | |
dc.language.iso | en | |
dc.publisher | National Academy of Sciences | |
dc.relation.url | http://www.pnas.org/cgi/content/full/104/9/3526 | |
dc.subject | Carbenicillin | |
dc.subject | Exopolymer | |
dc.subject | Motility | |
dc.subject | Desiccation | |
dc.subject | Nucleoid | |
dc.subject.mesh | Carbenicillin | |
dc.subject.mesh | Cell Membrane | |
dc.subject.mesh | Chromatography, Thin Layer | |
dc.subject.mesh | Microscopy, Electron | |
dc.subject.mesh | Mutagenesis | |
dc.subject.mesh | Mutation | |
dc.subject.mesh | Phosphotransferases (Phosphate Group Acceptor) | |
dc.subject.mesh | Pseudomonas aeruginosa | |
dc.title | A polyphosphate kinase 1 (ppk1) mutant of Pseudomonas aeruginosa exhibits multiple ultrastructural and functional defects. | |
dc.type | Journal article | |
dc.identifier.journal | Proceedings of the National Academy of Sciences of the United States of America | |
html.description.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. |