ArticleCommunications biology2023
A moonlighting role for LysM peptidoglycan binding domains underpins Enterococcus faecalis daughter cell separation.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Hidden diversity inMicrobiology spectrum · 2025Article
- Purification and Characterization of Enterocins A, B, and a Novel High-Mass Bacteriocin fromAntibiotics (Basel, Switzerland) · 2025Article
- Enterococcal cell wall remodelling underpins pathogenesis via the release of the Enteroccocal Polysaccharide Antigen (EPA).PLoS pathogens · 2025Article
- Genomic insights into the beneficial potential ofMicrobial genomics · 2025Article
- Exploring the genomic traits of infant-associated microbiota members from a Zimbabwean cohort.BMC genomics · 2024Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Control of cell size and morphology is of paramount importance for bacterial fitness. In the opportunistic pathogen Enterococcus faecalis, the formation of diplococci and short cell chains facilitates innate immune evasion and dissemination in the host. Minimisation of cell chain size relies on the activity of a peptidoglycan hydrolase called AtlA, dedicated to septum cleavage. To prevent autolysis, AtlA activity is tightly controlled, both temporally and spatially. Here, we show that the restricted localization of AtlA at the septum occurs via an unexpected mechanism. We demonstrate that the C-terminal LysM domain that allows the enzyme to bind peptidoglycan is essential to target this enzyme to the septum inside the cell before its translocation across the membrane. We identify a membrane-bound cytoplasmic protein partner (called AdmA) involved in the recruitment of AtlA via its LysM domains. This work reveals a moonlighting role for LysM domains, and a mechanism evolved to restrict the subcellular localization of a potentially lethal autolysin to its site of action.
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