A widespread family of bacterial cell wall assembly proteins

Yoshikazu Kawai, Jon Marles-Wright, Robert M Cleverley, Robyn Emmins, Shu Ishikawa, Masayoshi Kuwano, Nadja Heinz, Nhat Khai Bui, Christopher N Hoyland, Naotake Ogasawara, Richard J Lewis, Waldemar Vollmer, Richard A Daniel, Jeff Errington

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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.
Original languageEnglish
Pages (from-to)4931-4941
Number of pages11
JournalEMBO Journal
Issue number24
Publication statusPublished - Dec 2011

Keywords / Materials (for Non-textual outputs)

  • capsular polysaccharide
  • LytR–CpsA–Psr proteins
  • MreB
  • peptidoglycan
  • teichoic acids


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