Reference : The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of E...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/3609
The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia Coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure
English
Goffin, Colette mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Fraipont, Claudine mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Ayala, Juan [Universidad Autonoma (Madrid) > Consejo Superior de Investigaciones Cientificas > Centro de Biologia Molecular Severo Ochoa > >]
Terrak, Mohammed mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Sep-1996
Journal of Bacteriology
American Society for Microbiology (ASM)
178
18
5402-5409
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] The ftsI-encoded multimodular class B penicillin-binding protein 3 (PBP3) is a key element of the cell septation machinery of Escherichia coli. Altered ftsI genes were overexpressed, and the gene products were analyzed with respect to the level of production, stability, penicillin affinity, and cell septation activity. In contrast to the serine beta-lactamases and low-molecular-mass PBPs which are autonomous folding entities, the S-259-to-V-577 penicillin-binding module of M-1-to-V-577 PBP3 lacks the amino acid sequence information for correct folding. The missing piece of information is provided by the associated G-57-to-E-258 non-penicillin-binding module which functions as a noncleaved, pseudointramolecular chaperone. Key elements of the folding information reside within the motif 1-containing R-60-to-W-110 polypeptide segment and within G-188-to-D-197 motif 3 of the n-PB module. The intermodule interaction is discussed in the light of the known three-dimensional structure (at 3.5-A [0.35-nm] resolution) of the analogous class B PBP2x of Streptococcus pneumoniae (S. Pares, N. Mouz, Y. Petillot, R. Hakenbeck, and O. Dideberg, Nature Struct. Biol. 3:284-289, 1996). Correct folding and adoption of a stable penicillin-binding conformation are necessary but not sufficient to confer cell septation activity to PBP3 in exponentially growing cells. The in vivo activity of PBP3 also depends on the M-1-to-E-56 amino-terminal module which encompasses the cytosol, the membrane, and the periplasm and which functions as a noncleaved pseudo-signal peptide.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/3609

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