Affiliation:
1. Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom,1 and
2. Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria2
Abstract
ABSTRACT
The composition and fine structure of the vegetative cell wall peptidoglycan from
Bacillus subtilis
were determined by analysis of its constituent muropeptides. The structures of 39 muropeptides, representing 97% of the total peptidoglycan, were elucidated. About 99% analyzed muropeptides in
B. subtilis
vegetative cell peptidoglycan have the free carboxylic group of diaminopimelic acid amidated. Anhydromuropeptides and products missing a glucosamine at the nonreducing terminus account for 0.4 and 1.5%, respectively, of the total muropeptides. These two types of muropeptides are suggested to end glycan strands. An unexpected feature of
B. subtilis
muropeptides was the occurrence of a glycine residue in position 5 of the peptide side chain on monomers or oligomers, which account for 2.7% of the total muropeptides. This amount is, however, dependent on the composition of the growth media. Potential attachment sites for anionic polymers to peptidoglycan occur on dominant muropeptides and account for 2.1% of the total.
B. subtilis
peptidoglycan is incompletely digested by lysozyme due to de-N-acetylation of glucosamine, which occurs on 17.3% of muropeptides. The cross-linking index of the polymer changes with the growth phase. It is highest in late stationary phase, with a value of 33.2 or 44% per muramic acid residue, as determined by reverse-phase high-pressure liquid chromatography or gel filtration, respectively. Analysis of the muropeptide composition of a
dacA
(PBP 5) mutant shows a dramatic decrease of muropeptides with tripeptide side chains and an increase or appearance of muropeptides with pentapeptide side chains in monomers or oligomers. The total muropeptides with pentapeptide side chains accounts for almost 82% in the
dacA
mutant. This major low-molecular-weight PBP (
dd
-carboxypeptidase) is suggested to play a role in peptidoglycan maturation.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference46 articles.
1. Archibald
A. R.
Hancock
I. C.
Harwood
C. R.
Cell wall structure synthesis and turnover
Bacillus subtilis and other gram-positive bacteria biochemistry physiology and molecular genetics.
Hoch
J. A.
Losick
R.
1993
381
410
American Society for Microbiology
Washington D.C
2. Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation
3. Peptidoglycan Structural Dynamics during Germination of
Bacillus subtilis
168 Endospores
4. Structural analysis of Bacillus megaterium KM spores peptidoglycan and its dynamics during germination;Atrih A.;Microbiology,1999
5. The role of autolysins during vegetative growth of Bacillus subtilis 168;Blackman S. A.;Microbiology,1998
Cited by
211 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献