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Sci Rep. 2018 May 15;8(1):7591. doi: 10.1038/s41598-018-25882-y.

The cell wall hydrolase Pmp23 is important for assembly and stability of the division ring in Streptococcus pneumoniae.

Author information

1
Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, 38000, Grenoble, France.
2
Indiana University, Department of Biology, Bloomington, IN, 47405, USA.
3
Molecular Microbiology and Structural Biochemistry (MMSB), CNRS, University Lyon 1, UMR 5086, Lyon, 69007, France.
4
Northeastern University, Department of Biology, Boston, MA, 02115, USA.
5
Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
6
Laboratoire de Chimie Bactérienne, Institut de Microbiologie de la Méditerranée, University Aix-Marseille, CNRS, UMR7283, 13009, Marseille, France.
7
Indiana University, Departments of Biology and Chemistry, Bloomington, IN, 47405, USA.
8
Molecular Microbiology and Structural Biochemistry (MMSB), CNRS, University Lyon 1, UMR 5086, Lyon, 69007, France. christophe.grangeasse@ibcp.fr.
9
Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, 38000, Grenoble, France. cecile.morlot@ibs.fr.

Abstract

Bacterial division is intimately linked to synthesis and remodeling of the peptidoglycan, a cage-like polymer that surrounds the bacterial cell, providing shape and mechanical resistance. The bacterial division machinery, which is scaffolded by the cytoskeleton protein FtsZ, includes proteins with enzymatic, structural or regulatory functions. These proteins establish a complex network of transient functional and/or physical interactions which preserve cell shape and cell integrity. Cell wall hydrolases required for peptidoglycan remodeling are major contributors to this mechanism. Consistent with this, their deletion or depletion often results in morphological and/or division defects. However, the exact function of most of them remains elusive. In this work, we show that the putative lysozyme activity of the cell wall hydrolase Pmp23 is important for proper morphology and cell division in the opportunistic human pathogen Streptococcus pneumoniae. Our data indicate that active Pmp23 is required for proper localization of the Z-ring and the FtsZ-positioning protein MapZ. In addition, Pmp23 localizes to the division site and interacts directly with the essential peptidoglycan synthase PBP2x. Altogether, our data reveal a new regulatory function for peptidoglycan hydrolases.

PMID:
29765094
PMCID:
PMC5954120
DOI:
10.1038/s41598-018-25882-y
[Indexed for MEDLINE]
Free PMC Article

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