ArticleMolecular microbiology2013
FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.
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Who cites it
113 citing papers in PubMed, 173 citations in OpenAlex.
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- The multiple roles of the NlpC_P60 peptidase family in mycobacteria - an underexplored target for antimicrobial drug discovery.FEBS letters · 2025Review
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- Evidence that glycopolymer transferases promote peptidoglycan hydrolysis inbioRxiv : the preprint server for biology · 2025Article
- Identification of insertion sites for the integrative and conjugative element Tn916 in the Bacillus subtilis chromosome.PloS one · 2025Article
- Modulation of the lytic apparatus by the FtsEX complex within the bacterial division machinery.FEBS letters · 2024Review
- Transcription termination and antitermination are critical for the fitness and function of the integrative and conjugative element Tn916.PLoS genetics · 2024Article
- Outer membrane barrier impairment byMicrobiology (Reading, England) · 2024Article
- DnaA modulates the gene expression and morphology of the Lyme disease spirochete.bioRxiv : the preprint server for biology · 2024Article
- The characteristics of autolysins associated with cell separation inJournal of bacteriology · 2024Article
- Elongasome core proteins and class A PBP1a display zonal, processive movement at the midcell ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
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- Structure and activity of the septal peptidoglycan hydrolysis machinery crucial for bacterial cell division.PLoS biology · 2024Article
53 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The peptidoglycan (PG) sacculus, a meshwork of polysaccharide strands cross-linked by short peptides, protects bacterial cells against osmotic lysis. To enlarge this covalently closed macromolecule, PG hydrolases must break peptide cross-links in the meshwork to allow insertion of new glycan strands between the existing ones. In the rod-shaped bacterium Bacillus subtilis, cell wall elongation requires two redundant endopeptidases, CwlO and LytE. However, it is not known how these potentially autolytic enzymes are regulated to prevent lethal breaches in the cell wall. Here, we show that the ATP-binding cassette transporter-like FtsEX complex is required for CwlO activity. In Escherichia coli, FtsEX is thought to harness ATP hydrolysis to activate unrelated PG hydrolases during cell division. Consistent with this regulatory scheme, B. subtilis FtsE mutants that are unable to bind or hydrolyse ATP cannot activate CwlO. Finally, we show that in cells depleted of both CwlO and LytE, the PG synthetic machinery continues moving circumferentially until cell lysis, suggesting that cross-link cleavage is not required for glycan strand polymerization. Overall, our data support a model in which the FtsEX complex is a remarkably flexible regulatory module capable of controlling a diverse set of PG hydrolases during growth and division in different organisms.
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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.