Faculty Opinions recommendation of Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to beta-lactam agents.

2010 ◽  
Author(s):  
Samuel Kariuki
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Beta Lactam ◽  
Escherichia Coli Cells

scholarly journals Differential Responses of Escherichia coli Cells Expressing Cytoplasmic Domain Mutants of Penicillin-Binding Protein 1b after Impairment of Penicillin-Binding Proteins 1a and 3

2001 ◽  
Vol 183 (1) ◽  
pp. 200-206 ◽  
Author(s):  
Christian Chalut ◽  
Xavier Charpentier ◽  
Marie-Hélène Remy ◽  
Jean-Michel Masson
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Single Gene ◽  
Cytoplasmic Tail ◽  
Cytoplasmic Domain ◽  
Full Length ◽  
Specific Interactions ◽  
Penicillin Binding Protein ◽  
Penicillin Binding Proteins ◽  
Escherichia Coli Cells

ABSTRACT Penicillin-binding protein 1b (PBP1b) is the major high-molecular-weight PBP in Escherichia coli. Although it is coded by a single gene, it is usually found as a mixture of three isoforms which vary with regard to the length of their N-terminal cytoplasmic tail. We show here that although the cytoplasmic tail seems to play no role in the dimerization of PBP1b, as was originally suspected, only the full-length protein is able to protect the cells against lysis when both PBP1a and PBP3 are inhibited by antibiotics. This suggests a specific role for the full-length PBP1b in the multienzyme peptidoglycan-synthesizing complex that cannot be fulfilled by either PBP1a or the shorter PBP1b proteins. Moreover, we have shown by alanine-stretch-scanning mutagenesis that (i) residues R11 to G13 are major determinants for correct translocation and folding of PBP1b and that (ii) the specific interactions involving the full-length PBP1b can be ascribed to the first six residues at the N-terminal end of the cytoplasmic domain. These results are discussed in terms of the interactions with other components of the murein-synthesizing complex.

scholarly journals A new beta-lactam-binding protein derived from penicillin-binding protein 3 of Escherichia coli.

1989 ◽  
Vol 171 (9) ◽  
pp. 5194-5198 ◽  
Author(s):  
R Prats ◽  
M Gomez ◽  
J Pla ◽  
B Blasco ◽  
J A Ayala
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Beta Lactam
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