Reference : Monofunctional transglycosylases are not essential for Staphylococcus aureus cell wal...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/94685
Monofunctional transglycosylases are not essential for Staphylococcus aureus cell wall synthesis.
English
Reed, Patricia [> > > >]
Veiga, Helena [> > > >]
Jorge, Ana M [> > > >]
Terrak, Mohammed mailto [> > > >]
Pinho, Mariana G [> >]
2011
Journal of Bacteriology
American Society for Microbiology (ASM)
193
10
2549-56
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] 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.
Researchers ; Professionals
http://hdl.handle.net/2268/94685
also: http://hdl.handle.net/2268/94718
10.1128/JB.01474-10

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