PMID:11114917

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Citation

Chalut, C, Charpentier, X, Remy, MH and Masson, JM (2001) Differential responses of Escherichia coli cells expressing cytoplasmic domain mutants of penicillin-binding protein 1b after impairment of penicillin-binding proteins 1a and 3. J. Bacteriol. 183:200-6

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 R(11) to G(13) 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.

Links

PubMed PMC94866 Online version:10.1128/JB.183.1.200-206.2001

Keywords

Amino Acid Sequence; Anti-Bacterial Agents/pharmacology; Aztreonam/pharmacology; Bacterial Proteins; Carrier Proteins; Cephaloridine/pharmacology; Cephalosporins/pharmacology; Cytoplasm/enzymology; Dimerization; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Hexosyltransferases/chemistry; Hexosyltransferases/genetics; Hexosyltransferases/metabolism; Isoenzymes/chemistry; Isoenzymes/genetics; Isoenzymes/metabolism; Molecular Sequence Data; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Mutation; Penicillin-Binding Proteins; Peptidoglycan Glycosyltransferase; Peptidyl Transferases/chemistry; Peptidyl Transferases/genetics; Peptidyl Transferases/metabolism; Serine-Type D-Ala-D-Ala Carboxypeptidase

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