ArticleThe Journal of biological chemistry2012
Determinants of murein hydrolase targeting to cross-wall of Staphylococcus aureus peptidoglycan.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 92 citations in OpenAlex.
- Glycoepitopes of staphylococcal wall teichoic acid govern complement-mediated opsonophagocytosis via human serum antibody and mannose-binding lectin.The Journal of biological chemistry · 2013Trial
- Genome-wide screen identifies novel factors for surface protein cross-wall trafficking and cell envelope homeostasis inJournal of bacteriology · 2026Article
- A chimeric, half-life extended lysin with a unique mode of action.Frontiers in microbiology · 2026Article
- A new regulator of the Staphylococcus aureus peptidoglycan hydrolase Sle1.PLoS genetics · 2025Article
- Genome-wide screen identifies novel factors for surface protein cross-wall trafficking and cell envelope homeostasis inbioRxiv : the preprint server for biology · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Cell splitting in Staphylococcus aureus is controlled by an adaptor protein facilitating degradation of a peptidoglycan hydrolase.PLoS genetics · 2025Article
- Cryo-EM analyses unveil details of mechanism and targocil-II mediated inhibition of S. aureus WTA transporter TarGH.Nature communications · 2025Article
- Evidence that glycopolymer transferases promote peptidoglycan hydrolysis inbioRxiv : the preprint server for biology · 2025Article
- Noninvasive Analysis of Peptidoglycan from Living Animals.Bioconjugate chemistry · 2024Article
- Probing Bacterial Cell Division and Cell Envelope Biogenesis with Live-Cell Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cell division protein FtsK coordinates bacterial chromosome segregation and daughter cell separation in Staphylococcus aureus.The EMBO journal · 2023Article
- The cell cycle of Staphylococcus aureus: An updated review.MicrobiologyOpen · 2023Review
- Staphylococcus aureus cell wall maintenance - the multifaceted roles of peptidoglycan hydrolases in bacterial growth, fitness, and virulence.FEMS microbiology reviews · 2022Review
- GpsB Coordinates Cell Division and Cell Surface Decoration by Wall Teichoic Acids in Staphylococcus aureus.Microbiology spectrum · 2022Article
- Targeting the Holy Triangle of Quorum Sensing, Biofilm Formation, and Antibiotic Resistance in Pathogenic Bacteria.Microorganisms · 2022Review
- Design and characterization of a novel lytic protein against Clostridium difficile.Applied microbiology and biotechnology · 2022Article
- A CRISPR interference screen reveals a role for cell wall teichoic acids in conjugation in Bacillus subtilis.Molecular microbiology · 2022Article
- Impact ofMicroorganisms · 2022Article
- Synthetic antimicrobial peptides as enhancers of the bacteriolytic action of staphylococcal phage endolysins.Scientific reports · 2022Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cells of eukaryotic or prokaryotic origin express proteins with LysM domains that associate with the cell wall envelope of bacteria. The molecular properties that enable LysM domains to interact with microbial cell walls are not yet established. Staphylococcus aureus, a spherical microbe, secretes two murein hydrolases with LysM domains, Sle1 and LytN. We show here that the LysM domains of Sle1 and LytN direct murein hydrolases to the staphylococcal envelope in the vicinity of the cross-wall, the mid-cell compartment for peptidoglycan synthesis. LysM domains associate with the repeating disaccharide β-N-acetylmuramic acid, (1→4)-β-N-acetylglucosamine of staphylococcal peptidoglycan. Modification of N-acetylmuramic acid with wall teichoic acid, a ribitol-phosphate polymer tethered to murein linkage units, prevents the LysM domain from binding to peptidoglycan. The localization of LytN and Sle1 to the cross-wall is abolished in staphylococcal tagO mutants, which are defective for wall teichoic acid synthesis. We propose a model whereby the LysM domain ensures septal localization of LytN and Sle1 followed by processive cleavage of peptidoglycan, thereby exposing new LysM binding sites in the cross-wall and separating bacterial cells.
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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.