Newcastle University

A widespread family of bacterial cell wall assembly proteins

Yoshikazu Kawai¹, Jon Marles-Wright¹, Robert M Cleverley¹, Robyn Emmins¹, Shu Ishikawa², Masayoshi Kuwano², Nadja Heinz¹, Nhat Khai Bui¹, Christopher N Hoyland¹, Naotake Ogasawara², Richard J Lewis¹, Waldemar Vollmer¹, Richard A Daniel¹ and Jeff Errington¹

1. Centre for Bacterial Cell Biology, Medical School, Newcastle University, Newcastle upon Tyne, UK
2. Graduate School of Information Science, Nara Institute of Science and Technology, Nara, Japan

Correspondence to:

Jeff Errington, Centre for Bacterial Cell Biology, Medical School, Newcastle University, Richardson Road, Newcastle upon Tyne NE2 4AX, UK. Tel.: +44 191 222 8126; Fax: +44 191 222 7424; E-mail: jeff.errington@ncl.ac.uk

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.

Full Article: http://www.nature.com/emboj/journal/vaop/ncurrent/full/emboj2011358a.html