Document Detail


Monofunctional transglycosylases are not essential for Staphylococcus aureus cell wall synthesis.
MedLine Citation:
PMID:  21441517     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The polymerization of peptidoglycan is the result of two types of enzymatic activities: transglycosylation, the formation of linear glycan chains, and transpeptidation, the formation of peptide cross-bridges between the glycan strands. Staphylococcus aureus has four penicillin binding proteins (PBP1 to PBP4) with transpeptidation activity, one of which, PBP2, is a bifunctional enzyme that is also capable of catalyzing transglycosylation reactions. Additionally, two monofunctional transglycosylases have been reported in S. aureus: MGT, which has been shown to have in vitro transglycosylase activity, and a second putative transglycosylase, SgtA, identified only by sequence analysis. We have now shown that purified SgtA has in vitro transglycosylase activity and that both MGT and SgtA are not essential in S. aureus. However, in the absence of PBP2 transglycosylase activity, MGT but not SgtA becomes essential for cell viability. This indicates that S. aureus cells require one transglycosylase for survival, either PBP2 or MGT, both of which can act as the sole synthetic transglycosylase for cell wall synthesis. We have also shown that both MGT and SgtA interact with PBP2 and other enzymes involved in cell wall synthesis in a bacterial two-hybrid assay, suggesting that these enzymes may work in collaboration as part of a larger, as-yet-uncharacterized cell wall-synthetic complex.
Authors:
Patricia Reed; Helena Veiga; Ana M Jorge; Mohammed Terrak; Mariana G Pinho
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-03-25
Journal Detail:
Title:  Journal of bacteriology     Volume:  193     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-04-29     Completed Date:  2011-07-22     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2549-56     Citation Subset:  IM    
Affiliation:
Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República, Apartado 2781-901 Oeiras, Portugal.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins
Cell Wall / metabolism*
Gene Deletion
Genes, Essential
Hexosyltransferases
Microbial Viability
Penicillin-Binding Proteins / genetics,  metabolism
Peptidoglycan / metabolism*
Peptidoglycan Glycosyltransferase / genetics,  isolation & purification,  metabolism*
Protein Binding
Protein Interaction Mapping
Staphylococcus aureus / enzymology*,  genetics,  metabolism
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Penicillin-Binding Proteins; 0/Peptidoglycan; EC 2.4.1.-/Hexosyltransferases; EC 2.4.1.-/MGT protein, Staphylococcus aureus; EC 2.4.1.129/Peptidoglycan Glycosyltransferase
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