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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Abstract	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.
AbstractList	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. Genetic determinants and enzymes that catalyze the multiple steps in the assembly of bacterial cell wall peptidoglycan have been known for some time. On the other hand, the mechanism by which glutamic acid residues of this structure undergo modification to glutamine has remained unknown. In this communication, we describe the identification of two genetic determinants that appear to be responsible for the completion of the chemical structure of the cell wall of the important human pathogen S. aureus. The availability of a conditional mutant which allows modulation of this system has allowed us to recognize the importance of glutamine residues for optimal growth rate and drug resistance and sensitivity of the staphylococcal peptidoglycan to the host defense factor lysozyme. 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. 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. 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.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	Sobral, Rita G. Vollmer, Waldemar de Almeida, João Manuel Feio Bui, Nhat K. Ludovice, Ana Madalena Tomasz, Alexander de Lencastre, Hermínia Figueiredo, Teresa A.
AuthorAffiliation	2 Centro de Recursos Microbiológicos (CREM), Departamento de Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Quinta da Torre, Caparica, Portugal 4 Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom 5 The Rockefeller University, Laboratory of Microbiology, New York, New York, United States of America Dartmouth Medical School, United States of America 3 Departamento de Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Quinta da Torre, Caparica, Portugal 1 Laboratory of Molecular Genetics, Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa, Oeiras, Portugal
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BackLink	https://www.ncbi.nlm.nih.gov/pubmed/22303291$$D View this record in MEDLINE/PubMed
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Copyright	2012 Figueiredo et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Figueiredo TA, Sobral RG, Ludovice AM, de Almeida JMF, Bui NK, et al. (2012) Identification of Genetic Determinants and Enzymes Involved with the Amidation of Glutamic Acid Residues in the Peptidoglycan of Staphylococcus aureus. PLoS Pathog 8(1): e1002508. doi:10.1371/journal.ppat.1002508 Figueiredo et al. 2012
Copyright_xml	– notice: 2012 Figueiredo et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Figueiredo TA, Sobral RG, Ludovice AM, de Almeida JMF, Bui NK, et al. (2012) Identification of Genetic Determinants and Enzymes Involved with the Amidation of Glutamic Acid Residues in the Peptidoglycan of Staphylococcus aureus. PLoS Pathog 8(1): e1002508. doi:10.1371/journal.ppat.1002508 – notice: Figueiredo et al. 2012
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Keywords	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
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Notes	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.
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Snippet	The glutamic acid residues of the peptidoglycan of Staphylococcus aureus and many other bacteria become amidated by an as yet unknown mechanism. In this... The glutamic acid residues of the peptidoglycan of Staphylococcus aureus and many other bacteria become amidated by an as yet unknown mechanism. In this...
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SubjectTerms	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
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Title	Identification of Genetic Determinants and Enzymes Involved with the Amidation of Glutamic Acid Residues in the Peptidoglycan of Staphylococcus aureus
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