FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens.

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Version: author
Serval ID
serval:BIB_63D5FE5C5A01
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens.
Journal
Nature Communications
Author(s)
Frandi A., Jacquier N., Théraulaz L., Greub G., Viollier P.H.
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Publication state
Published
Issued date
2014
Peer-reviewed
Oui
Volume
5
Pages
4200
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: epublish
Abstract
The nature and assembly of the chlamydial division septum is poorly defined due to the paucity of a detectable peptidoglycan (PG)-based cell wall, the inhibition of constriction by penicillin and the presence of coding sequences for cell wall precursor and remodelling enzymes in the reduced chlamydial (pan-)genome. Here we show that the chlamydial amidase (AmiA) is active and remodels PG in Escherichia coli. Moreover, forward genetics using an E. coli amidase mutant as entry point reveals that the chlamydial LysM-domain protein NlpD is active in an E. coli reporter strain for PG endopeptidase activity (ΔnlpI). Immunolocalization unveils NlpD as the first septal (cell-wall-binding) protein in Chlamydiae and we show that its septal sequestration depends on prior cell wall synthesis. Since AmiA assembles into peripheral clusters, trimming of a PG-like polymer or precursors occurs throughout the chlamydial envelope, while NlpD targets PG-like peptide crosslinks at the chlamydial septum during constriction.
Pubmed
Web of science
Open Access
Yes
Create date
05/08/2014 17:55
Last modification date
20/08/2019 14:20
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