Identification of Genetic Determinants and Enzymes Involved with the Amidation of Glutamic Acid Residues in the Peptidoglycan of Staphylococcus aureus

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 responsi...

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Vydáno v:	PLoS pathogens Ročník 8; číslo 1; s. e1002508
Hlavní autoři:	Figueiredo, Teresa A., Sobral, Rita G., Ludovice, Ana Madalena, de Almeida, João Manuel Feio, Bui, Nhat K., Vollmer, Waldemar, de Lencastre, Hermínia, Tomasz, Alexander
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Public Library of Science 01.01.2012 Public Library of Science (PLoS)
Témata:	Amidohydrolases - genetics Amidohydrolases - metabolism Amino Acid Sequence Antibiotics Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biology Biosynthesis Blotting, Northern Chromatography, High Pressure Liquid Drug resistance Enzymes Experiments Genes, Bacterial - genetics Genomes Glutamic Acid - metabolism Gram-positive bacteria Growth rate Lipids Mass Spectrometry Microbiology Molecular Sequence Data Peptides Peptidoglycan - metabolism Plasmids Reverse Transcriptase Polymerase Chain Reaction Staphylococcus aureus - genetics Staphylococcus aureus - metabolism Amidohydrolases Glutamic Acid Amino Acid Sequence Genes, Bacterial Peptidoglycan Blotting, Northern Mass Spectrometry Molecular Sequence Data Chromatography, High Pressure Liquid Reverse Transcriptase Polymerase Chain Reaction Staphylococcus aureus Bacterial Proteins
ISSN:	1553-7374, 1553-7366, 1553-7374
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Shrnutí:	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.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Conceived and designed the experiments: RGS AML WV HdL AT. Performed the experiments: TAF RGS NKB. Analyzed the data: RGS TAF AML WV HdL AT. Bioinformatic analysis: JMFA. Wrote the paper: RGS TAF AML WV HdL AT.
ISSN:	1553-7374 1553-7366 1553-7374
DOI:	10.1371/journal.ppat.1002508