Pentapeptide-rich peptidoglycan at the Bacillus subtilis cell-division site.

Details

Serval ID
serval:BIB_FA1EB32ACDE7
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Pentapeptide-rich peptidoglycan at the Bacillus subtilis cell-division site.
Journal
Molecular Microbiology
Author(s)
Morales Angeles D., Liu Y., Hartman A.M., Borisova M., de Sousa Borges A., de Kok N., Beilharz K., Veening J.W., Mayer C., Hirsch A.K., Scheffers D.J.
ISSN
1365-2958 (Electronic)
ISSN-L
0950-382X
Publication state
Published
Issued date
2017
Peer-reviewed
Oui
Volume
104
Number
2
Pages
319-333
Language
english
Abstract
Peptidoglycan (PG), the major component of the bacterial cell wall, is one large macromolecule. To allow for the different curvatures of PG at cell poles and division sites, there must be local differences in PG architecture and eventually also chemistry. Here we report such local differences in the Gram-positive rod-shaped model organism Bacillus subtilis. Single-cell analysis after antibiotic treatment and labeling of the cell wall with a fluorescent analogue of vancomycin or the fluorescent D-amino acid analogue (FDAA) HCC-amino-D-alanine revealed that PG at the septum contains muropeptides with unprocessed stem peptides (pentapeptides). Whereas these pentapeptides are normally shortened after incorporation into PG, this activity is reduced at division sites indicating either a lower local degree of PG crosslinking or a difference in PG composition, which could be a topological marker for other proteins. The pentapeptides remain partially unprocessed after division when they form the new pole of a cell. The accumulation of unprocessed PG at the division site is not caused by the activity of the cell division specific penicillin-binding protein 2B. To our knowledge, this is the first indication of local differences in the chemical composition of PG in Gram-positive bacteria.

Pubmed
Web of science
Open Access
Yes
Create date
02/02/2017 15:18
Last modification date
20/08/2019 16:25
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