Document Detail


Cell wall peptidoglycan architecture in Bacillus subtilis.
MedLine Citation:
PMID:  18784364     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Emma J Hayhurst; Lekshmi Kailas; Jamie K Hobbs; Simon J Foster
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-09-10
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  105     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2008 Sep 
Date Detail:
Created Date:  2008-09-24     Completed Date:  2008-10-22     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  14603-8     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Bacillus subtilis / chemistry*,  cytology*,  genetics
Bacterial Proteins / genetics
Cell Wall / chemistry*
Chromatography, Gel
Microscopy, Atomic Force
Models, Biological
Mutation
Peptidoglycan / chemistry*
Grant Support
ID/Acronym/Agency:
GR077544AIA//Wellcome Trust; //Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/MreC protein, Bacteria; 0/Peptidoglycan
Comments/Corrections

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