Format

Send to

Choose Destination
Mol Microbiol. 2017 Nov;106(3):419-438. doi: 10.1111/mmi.13775. Epub 2017 Sep 14.

LytM factors affect the recruitment of autolysins to the cell division site in Caulobacter crescentus.

Author information

1
Faculty of Biology, Philipps-Universität, Marburg 35043, Germany.
2
Max Planck Institute for Terrestrial Microbiology, Marburg 35043, Germany.
3
Divison of Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
4
Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
5
LOEWE Center for Synthetic Microbiology, Marburg 35043, Germany.

Abstract

Most bacteria possess a peptidoglycan cell wall that determines their morphology and provides mechanical robustness during osmotic challenges. The biosynthesis of this structure is achieved by a large set of synthetic and lytic enzymes with varying substrate specificities. Although the biochemical functions of these proteins are conserved and well-investigated, the precise roles of individual factors and the regulatory mechanisms coordinating their activities in time and space remain incompletely understood. Here, we comprehensively analyze the autolytic machinery of the alphaproteobacterial model organism Caulobacter crescentus, with a specific focus on LytM-like endopeptidases, soluble lytic transglycosylases and amidases. Our data reveal a high degree of redundancy within each protein family but also specialized functions for individual family members under stress conditions. In addition, we identify two lytic transglycosylases and an amidase as new divisome components that are recruited to midcell at distinct stages of the cell cycle. The midcell localization of these proteins is affected by two LytM factors with degenerate catalytic domains, DipM and LdpF, which may serve as regulatory hubs coordinating the activities of multiple autolytic enzymes during cell constriction and fission respectively. These findings set the stage for in-depth studies of the molecular mechanisms that control peptidoglycan remodeling in C. crescentus.

PMID:
28833791
DOI:
10.1111/mmi.13775
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center