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

Scientific Reports
Maxime JacqCécile Morlot

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 regu...Continue Reading

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Citations

Nov 20, 2019·ACS Chemical Biology·Erkin KuruMichael S VanNieuwenhze
Sep 4, 2021·Proceedings of the National Academy of Sciences of the United States of America·Atsushi TaguchiSuzanne Walker
Sep 17, 2021·Proceedings of the National Academy of Sciences of the United States of America·Joshua D Shirley, Erin E Carlson

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Methods Mentioned

BETA
fluorescence microscopy
electron microscopy
pull-down
immunoprecipitation
microscale thermophoresis
fluorescence microcopy
gel filtration
Assay

Software Mentioned

Prism7
MicrobeTracker Matlab
GraphPad
QMEAN

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