Cell wall peptidoglycan architecture in Bacillus subtilis.
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.
Hayhurst
Emma J
EJ
Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom.
Kailas
Lekshmi
L
Hobbs
Jamie K
JK
Foster
Simon J
SJ
D001412:Bacillus subtilis / Q000737:chemistry* / Q000166:cytology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics; D002473:Cell Wall / Q000737:chemistry*; D002850:Chromatography, Gel; D018625:Microscopy, Atomic Force; D008954:Models, Biological; D009154:Mutation; D010457:Peptidoglycan / Q000737:chemistry*
D001426:Bacterial Proteins; C062061:MreC protein, Bacteria; D010457:Peptidoglycan
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