title: Cell wall peptidoglycan architecture in Bacillus subtilis.
abstract: 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.affiliation: Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom.
authors.forename: Emma J
authors.initials: EJ
authors.lastname: Hayhurst
authors.forename: Lekshmi
authors.initials: L
authors.lastname: Kailas
authors.forename: Jamie K
authors.initials: JK
authors.lastname: Hobbs
authors.forename: Simon J
authors.initials: SJ
authors.lastname: Foster
mesh_terms: 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*
chemical_list: D001426:Bacterial Proteins; C062061:MreC protein, Bacteria; D010457:Peptidoglycan
references.citation: Microbiology (Reading). 2000 Feb;146 ( Pt 2):249-262
references.pmid: 10708363
references.citation: J Bacteriol. 1978 Nov;136(2):723-9
references.pmid: 361720
references.citation: Arch Microbiol. 1976 Aug;109(1-2):195-7
references.pmid: 822796
references.citation: J Bacteriol. 1999 Jul;181(13):3956-66
references.pmid: 10383963
references.citation: Nature. 1977 Mar 31;266(5601):450-2
references.pmid: 404566
references.citation: J Bacteriol. 2003 Jun;185(11):3458-68
references.pmid: 12754246
references.citation: J Bacteriol. 1980 Jan;141(1):327-32
references.pmid: 6986361
references.citation: J Infect Dis. 2006 Apr 15;193(8):1098-108
references.pmid: 16544250
references.citation: J Bacteriol. 1990 Jul;172(7):3758-71
references.pmid: 2361946
references.citation: J Bacteriol. 1976 Mar;125(3):1127-38
references.pmid: 815238
references.citation: J Infect Dis. 1973 Jul;128:Suppl:9-16
references.pmid: 4578317
references.citation: Res Microbiol. 1998 Nov-Dec;149(10):689-701
references.pmid: 9921576
references.citation: J Bacteriol. 2006 Sep;188(18):6652-60
references.pmid: 16952957
references.citation: Cell. 2003 Jun 13;113(6):767-76
references.pmid: 12809607
references.citation: Appl Environ Microbiol. 1990 Jul;56(7):2245-7
references.pmid: 1697149
references.citation: Mol Microbiol. 2007 Jul;65(1):180-200
references.pmid: 17581128
references.citation: Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4404-9
references.pmid: 16537437
references.citation: Biochem J. 1973 Jun;133(2):395-8
references.pmid: 4198851
references.citation: Mol Microbiol. 1998 Apr;28(2):235-47
references.pmid: 9622350
references.citation: J Bacteriol. 2004 Jun;186(11):3286-95
references.pmid: 15150213
references.citation: J Biol Chem. 2000 Apr 7;275(14):9910-8
references.pmid: 10744664
references.citation: Anal Biochem. 1988 Aug 1;172(2):451-64
references.pmid: 3056100
references.citation: J Bacteriol. 2004 Nov;186(21):7141-8
references.pmid: 15489425
references.citation: Mol Microbiol. 2005 Sep;57(5):1196-209
references.pmid: 16101995
references.citation: Nat Struct Biol. 2002 Nov;9(11):870-6
references.pmid: 12389036
references.citation: J Bacteriol. 1975 Nov;124(2):905-17
references.pmid: 1184577
references.citation: Arch Biochem Biophys. 1976 Nov;177(1):330-3
references.pmid: 999292
references.citation: Anal Biochem. 1990 Oct;190(1):120-8
references.pmid: 2285138
references.citation: Biopolymers. 1987 Aug;26(8):1391-406
references.pmid: 3663868
references.citation: J Bacteriol. 2004 Sep;186(18):5978-87
references.pmid: 15342566
references.citation: Proc Natl Acad Sci U S A. 1976 May;73(5):1740-4
references.pmid: 818642
references.citation: Ultramicroscopy. 2004 Nov;101(2-4):105-9
references.pmid: 15450655
references.citation: Mol Microbiol. 2005 Apr;56(1):240-51
references.pmid: 15773993
references.citation: Proc Natl Acad Sci U S A. 2007 Jun 5;104(23):9644-9
references.pmid: 17535925