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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
2008-9-24
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pubmed:abstractText |
The bacterial cell wall is essential for viability and shape determination. Cell wall structural dynamics allowing growth and division, while maintaining integrity is a basic problem governing the life of bacteria. The polymer peptidoglycan is the main structural component for most bacteria and is made up of glycan strands that are cross-linked by peptide side chains. Despite study and speculation over many years, peptidoglycan architecture has remained largely elusive. Here, we show that the model rod-shaped bacterium Bacillus subtilis has glycan strands up to 5 microm, longer than the cell itself and 50 times longer than previously proposed. Atomic force microscopy revealed the glycan strands to be part of a peptidoglycan architecture allowing cell growth and division. The inner surface of the cell wall has a regular macrostructure with approximately 50 nm-wide peptidoglycan cables [average 53 +/- 12 nm (n = 91)] running basically across the short axis of the cell. Cross striations with an average periodicity of 25 +/- 9 nm (n = 96) along each cable are also present. The fundamental cabling architecture is also maintained during septal development as part of cell division. We propose a coiled-coil model for peptidoglycan architecture encompassing our data and recent evidence concerning the biosynthetic machinery for this essential polymer.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-10383963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-10744664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-1184577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-12389036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-12754246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-12809607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-15150213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-15342566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-15450655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-15489425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-15773993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-16101995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-16537437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-16544250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-16952957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-1697149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-17535925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-17581128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-2285138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-2361946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-3056100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-361720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-3663868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-404566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-4198851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-4578317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-6986361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-815238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-818642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-822796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-9622350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-9921576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18784364-999292
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14603-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18784364-Bacillus subtilis,
pubmed-meshheading:18784364-Bacterial Proteins,
pubmed-meshheading:18784364-Cell Wall,
pubmed-meshheading:18784364-Chromatography, Gel,
pubmed-meshheading:18784364-Microscopy, Atomic Force,
pubmed-meshheading:18784364-Models, Biological,
pubmed-meshheading:18784364-Mutation,
pubmed-meshheading:18784364-Peptidoglycan
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pubmed:year |
2008
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pubmed:articleTitle |
Cell wall peptidoglycan architecture in Bacillus subtilis.
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pubmed:affiliation |
Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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