ArticleScientific reports2018
The cell wall hydrolase Pmp23 is important for assembly and stability of the division ring in Streptococcus pneumoniae.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025Review
- Article
- CRISPRi-TnSeq maps genome-wide interactions between essential and non-essential genes in bacteria.Nature microbiology · 2024Article
- Masters of Misdirection: Peptidoglycan Glycosidases in Bacterial Growth.Journal of bacteriology · 2023Review
- Inhibition ofMicrobiology (Reading, England) · 2022Article
- Looks can be deceiving: Bacterial enzymes work through unanticipated mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Biochemical reconstitution defines new functions for membrane-bound glycosidases in assembly of the bacterial cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Pneumococcal Divisome: Dynamic Control ofFrontiers in microbiology · 2021Review
- Mechanisms of Incorporation for D-Amino Acid Probes That Target Peptidoglycan Biosynthesis.ACS chemical biology · 2019Article
Corrections and comments
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Authors and funding
16 authors at 4 institutions in 3 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.