ArticleThe Journal of biological chemistry2011
LytN, a murein hydrolase in the cross-wall compartment of Staphylococcus aureus, is involved in proper bacterial growth and envelope assembly.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 80 citations in OpenAlex.
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- Signal peptidase SpsB coordinates staphylococcal cell cycle, surface protein septal trafficking and LTA synthesis.bioRxiv : the preprint server for biology · 2024Article
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- Tracking Cell Wall-Anchored Proteins in Gram-Positive Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The cell cycle of Staphylococcus aureus: An updated review.MicrobiologyOpen · 2023Review
- Coupling Novel Probes with Molecular Localization Microscopy Reveals Cell Wall Homeostatic Mechanisms inACS chemical biology · 2022Article
- Staphylococcus aureus cell wall maintenance - the multifaceted roles of peptidoglycan hydrolases in bacterial growth, fitness, and virulence.FEMS microbiology reviews · 2022Review
- Demonstration of the role of cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Peptidoglycan Contribution to the B Cell Superantigen Activity of Staphylococcal Protein A.mBio · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cell cycle progression for the spherical microbe Staphylococcus aureus requires the coordinated synthesis and remodeling of peptidoglycan. The majority of these rearrangements takes place at the mid-cell, in a compartment designated the cross-wall. Secreted polypeptides endowed with a YSIRK-G/S signal peptide are directly delivered to the cross-wall compartment. One such YSIRK-containing protein is the murein hydrolase LytN. lytN mutations precipitate structural damage to the cross-wall and interfere with staphylococcal growth. Overexpression of lytN also affects growth and triggers rupture of the cross-wall. The lytN phenotype can be reversed by the controlled expression of lytN but not by adding purified LytN to staphylococcal cultures. LytN harbors LysM and CHAP domains, the latter of which functions as both an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine endopeptidase. Thus, LytN secretion into the cross-wall promotes peptidoglycan separation and completion of the staphylococcal cell cycle.
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Registered trials
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