Skip to Main content Skip to Navigation
Journal articles

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

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.
Document type :
Journal articles
Complete list of metadatas

https://hal-amu.archives-ouvertes.fr/hal-01893223
Contributor : Delphine Leroi <>
Submitted on : Thursday, October 11, 2018 - 11:15:21 AM
Last modification on : Tuesday, November 3, 2020 - 3:14:25 PM

Links full text

Identifiers

Collections

Citation

Maxime Jacq, Christopher Arthaud, Sylvie Manuse, Chryslène Mercy, Laure Bellard, et al.. The cell wall hydrolase Pmp23 is important for assembly and stability of the division ring in Streptococcus pneumoniae. Scientific Reports, Nature Publishing Group, 2018, 8 (1), ⟨10.1038/s41598-018-25882-y⟩. ⟨hal-01893223⟩

Share

Metrics

Record views

407