Reference : PBP5 complementation of a PBP3 deficiency in Enterococcus hirae
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/63361
PBP5 complementation of a PBP3 deficiency in Enterococcus hirae
English
Leimanis, S. [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Hoyez, N. [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Hubert, S [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Laschet, M. [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Brasseur, Robert mailto [Faculté Universitaire des Sciences Agronomiques de Gembloux - FUSAGx > > > >]
Coyette, Jacques mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Sep-2006
Journal of Bacteriology
Amer Soc Microbiology
188
17
6298-6307
Yes (verified by ORBi)
International
0021-9193
Washington
[en] The low susceptibility of enterococci to beta-lactams is due to the activity of the low-affinity penicillin-binding protein 5 (PBP5). One important feature of PBP5 is its ability to substitute for most, if not all, penicillin-binding proteins when they are inhibited. That substitution activity was analyzed in Enterococcus hirae SL2, a mutant whose pbp5 gene was interrupted by the nisRK genes and whose PBP3 synthesis was submitted to nisin induction. Noninduced SL2 cells were unable to divide except when plasmid-borne pbp5 genes were present, provided that the PBP5 active site was functional. Potential protein-protein interaction sites of the PBP5 N-terminal module were mutagenized by site-directed mutagenesis. The T-167-L-184 region (designated site D) appeared to be an essential intramolecular site needed for the stability of the protein. Mutations made in the two globular domains present in the N-terminal module indicated that they were needed for the suppletive activity. The P-197-N-209 segment (site E) in one of these domains seemed to be particularly important, as single and double mutations reduced or almost completely abolished, respectively, the action of PBP5.
Researchers ; Professionals
http://hdl.handle.net/2268/63361
also: http://hdl.handle.net/2268/125307
10.1128/JB.00334-06

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