Browse by author
Lookup NU author(s): Dr Nhat Khai Bui, Professor Waldemar Vollmer
The glutamic acid residues of the peptidoglycan of Staphylococcus aureus and many other bacteria become amidated by an as yet unknown mechanism. In this communication we describe the identification, in the genome of S. aureus strain COL, of two co-transcribed genes, murT and gatD, which are responsible for peptidoglycan amidation. MurT and GatD have sequence similarity to substrate-binding domains in Mur ligases (MurT) and to the catalytic domain in CobB/CobQ-like glutamine amidotransferases (GatD). The amidation of glutamate residues in the stem peptide of S. aureus peptidoglycan takes place in a later step than the cytoplasmic phase - presumably the lipid phase - of the biosynthesis of the S. aureus cell wall precursor. Inhibition of amidation caused reduced growth rate, reduced resistance to beta-lactam antibiotics and increased sensitivity to lysozyme which inhibited culture growth and caused degradation of the peptidoglycan.
Author(s): Figueiredo TA, Sobral RG, Ludovice AM, de Almeida JMF, Bui NK, Vollmer W, de Lencastre H, Tomasz A
Publication type: Article
Publication status: Published
Journal: PLoS Pathogens
Year: 2012
Volume: 8
Issue: 1
Print publication date: 26/01/2012
Date deposited: 29/03/2012
ISSN (print): 1553-7366
ISSN (electronic): 1553-7374
Publisher: Public Library of Science
URL: http://dx.doi.org/10.1371/journal.ppat.1002508
DOI: 10.1371/journal.ppat.1002508
Altmetrics provided by Altmetric