Two New M23 Peptidoglycan Hydrolases With Distinct Net Charge
Bacterial peptidoglycan hydrolases play an essential role in cell wall metabolism during bacterial growth, division, and elongation (autolysins) or in the elimination of closely related species from the same ecological niche (bacteriocins). Most studies concerning the peptidoglycan hydrolases presen...
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Published in | Frontiers in microbiology Vol. 12; p. 719689 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Frontiers Media S.A
24.09.2021
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Subjects | |
Online Access | Get full text |
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Summary: | Bacterial peptidoglycan hydrolases play an essential role in cell wall metabolism during bacterial growth, division, and elongation (autolysins) or in the elimination of closely related species from the same ecological niche (bacteriocins). Most studies concerning the peptidoglycan hydrolases present in Gram-positive bacteria have focused on clinically relevant
Staphylococcus aureus
or the model organism
Bacillus subtilis
, while knowledge relating to other species remains limited. Here, we report two new peptidoglycan hydrolases from the M23 family of metallopeptidases derived from the same staphylococcal species,
Staphylococcus pettenkoferi
. They share modular architecture, significant sequence identity (60%), catalytic and binding residue conservation, and similar modes of activation, but differ in gene distribution, putative biological role, and, strikingly, in their isoelectric points (pIs). One of the peptides has a high pI, similar to that reported for all M23 peptidases evaluated to date, whereas the other displays a low pI, a unique feature among M23 peptidases. Consequently, we named them SpM23_B (Staphylococcus pettenkoferi M23 “Basic”) and SpM23_A (Staphylococcus pettenkoferi M23 “Acidic”). Using genetic and biochemical approaches, we have characterized these two novel lytic enzymes, both
in vitro
and in their physiological context. Our study presents a detailed characterization of two novel and clearly distinct peptidoglycan hydrolases to understand their role in bacterial physiology. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Edited by: Ansgar Poetsch, Ruhr University Bochum, Germany This article was submitted to Microbial Physiology and Metabolism, a section of the journal Frontiers in Microbiology Reviewed by: Anthony J. Clarke, University of Guelph, Canada; Maria Cecilia Mansilla, CONICET Instituto de Biología Molecular y Celular de Rosario (IBR), Argentina |
ISSN: | 1664-302X 1664-302X |
DOI: | 10.3389/fmicb.2021.719689 |