Article (Scientific journals)
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
Goffin, Colette; Fraipont, Claudine; Ayala, Juan et al.
1996In Journal of Bacteriology, 178 (18), p. 5402-5409
Peer Reviewed verified by ORBi
 

Files


Full Text
Goffin_1996_J-Bact_5402.pdf
Author postprint (325.37 kB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Abstract :
[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.
Research center :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Microbiology
Biochemistry, biophysics & molecular biology
Author, co-author :
Goffin, Colette ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Fraipont, Claudine ;  Université de Liège - ULiège > 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  ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Nguyen-Distèche, Martine ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Language :
English
Title :
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
Publication date :
September 1996
Journal title :
Journal of Bacteriology
ISSN :
0021-9193
eISSN :
1098-5530
Publisher :
American Society for Microbiology (ASM), Washington, United States - District of Columbia
Volume :
178
Issue :
18
Pages :
5402-5409
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRFC - Fonds de la Recherche Fondamentale Collective [BE]
Available on ORBi :
since 06 January 2009

Statistics


Number of views
77 (13 by ULiège)
Number of downloads
114 (0 by ULiège)

Scopus citations®
 
38
Scopus citations®
without self-citations
29
OpenCitations
 
36

Bibliography


Similar publications



Contact ORBi