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A widespread family of bacterial cell wall assembly proteins
Author(s) -
Kawai Yoshikazu,
MarlesWright Jon,
Cleverley Robert M,
Emmins Robyn,
Ishikawa Shu,
Kuwano Masayoshi,
Heinz Nadja,
Bui Nhat Khai,
Hoyland Christopher N,
Ogasawara Naotake,
Lewis Richard J,
Vollmer Waldemar,
Daniel Richard A,
Errington Jeff
Publication year - 2011
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2011.358
Subject(s) - newcastle upon tyne , wright , library science , newcastle disease , medical school , media studies , sociology , biology , art history , art , medicine , medical education , computer science , genetics , virus
Teichoic acids and acidic capsular polysaccharides are major anionic cell wall polymers (APs) in many bacteria, with various critical cell functions, including maintenance of cell shape and structural integrity, charge and cation homeostasis, and multiple aspects of pathogenesis. We have identified the widespread LytR–Cps2A–Psr (LCP) protein family, of previously unknown function, as novel enzymes required for AP synthesis. Structural and biochemical analysis of several LCP proteins suggest that they carry out the final step of transferring APs from their lipid‐linked precursor to cell wall peptidoglycan (PG). In Bacillus subtilis , LCP proteins are found in association with the MreB cytoskeleton, suggesting that MreB proteins coordinate the insertion of the major polymers, PG and AP, into the cell wall.