<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zhang H</submitter><funding>NIGMS NIH HHS</funding><funding>U.S. Department of Health &amp;amp; Human Services | National Institutes of Health</funding><pagination>5357</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10475089</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(1)</volume><pubmed_abstract>Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion. However, the mechanisms of their coordination remain elusive. Moenomycin that inhibits a family of PG synthases known as Class-A penicillin-binding proteins (aPBPs), collapses rod shape despite aPBPs being non-essential for rod-like morphology in the bacterium Myxococcus xanthus. Here, we demonstrate that inhibited PBP1a2, an aPBP, accelerates the degradation of cell poles by DacB, a hydrolytic PG peptidase. Moenomycin promotes the binding between DacB and PG and thus reduces the mobility of DacB through PBP1a2. Conversely, DacB also regulates </pubmed_abstract><journal>Nature communications</journal><pubmed_title>Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall.</pubmed_title><pmcid>PMC10475089</pmcid><funding_grant_id>R01GM129000</funding_grant_id><funding_grant_id>R01 GM129000</funding_grant_id><pubmed_authors>Nan B</pubmed_authors><pubmed_authors>Zhang H</pubmed_authors><pubmed_authors>Ng E</pubmed_authors><pubmed_authors>Venkatesan S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall.</name><description>Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion. However, the mechanisms of their coordination remain elusive. Moenomycin that inhibits a family of PG synthases known as Class-A penicillin-binding proteins (aPBPs), collapses rod shape despite aPBPs being non-essential for rod-like morphology in the bacterium Myxococcus xanthus. Here, we demonstrate that inhibited PBP1a2, an aPBP, accelerates the degradation of cell poles by DacB, a hydrolytic PG peptidase. Moenomycin promotes the binding between DacB and PG and thus reduces the mobility of DacB through PBP1a2. Conversely, DacB also regulates </description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Sep</publication><modification>2025-05-29T21:44:41.524Z</modification><creation>2025-02-18T23:56:22.122Z</creation></dates><accession>S-EPMC10475089</accession><cross_references><pubmed>37660104</pubmed><doi>10.1038/s41467-023-41082-3</doi></cross_references></HashMap>