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

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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Morales Angeles D,Liu Y,Hartman AM,Borisova M,de Sousa Borges A,de Kok N,Beilharz K,Veening JW,Mayer C,Hirsch AK,Scheffers DJ

doi

10.1111/mmi.13629

subject

Has Abstract

pub_date

2017-04-01 00:00:00

pages

319-333

issue

2

eissn

0950-382X

issn

1365-2958

journal_volume

104

pub_type

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