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- W3011945425 abstract "Cell walls are barriers found in almost all known bacterial cells. These structures establish a controlled interface between the external environment and vital cellular components. A primary component of cell wall is a highly cross-linked matrix called peptidoglycan (PG). PG cross-linking, carried out by transglycosylases and transpeptidases, is necessary for proper cell wall assembly. Transpeptidases, targets of β-lactam antibiotics, stitch together two neighboring PG stem peptides (acyl-donor and acyl-acceptor strands). We recently described a novel class of cellular PG probes that were processed exclusively as acyl-donor strands. Herein, we have accessed the other half of the transpeptidase reaction by developing probes that are processed exclusively as acyl-acceptor strands. The critical nature of the cross-bridge on the PG peptide was demonstrated in live bacterial cells, and surprising promiscuity in cross-bridge primary sequence was found in various bacterial species. Additionally, acyl-acceptor probes provided insight into how chemical remodeling of the PG cross-bridge (e.g., amidation) can modulate cross-linking levels, thus establishing a physiological role of PG structural variations. Together, the acyl-donor and -acceptor probes will provide a versatile platform to interrogate PG cross-linking in physiologically relevant settings." @default.
- W3011945425 created "2020-03-23" @default.
- W3011945425 creator A5025721506 @default.
- W3011945425 creator A5039005001 @default.
- W3011945425 creator A5081309101 @default.
- W3011945425 date "2020-03-13" @default.
- W3011945425 modified "2023-09-30" @default.
- W3011945425 title "Remodeling of Cross-bridges Controls Peptidoglycan Cross-linking Levels in Bacterial Cell Walls" @default.
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- W3011945425 doi "https://doi.org/10.1021/acschembio.0c00002" @default.
- W3011945425 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7887760" @default.
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