A gene fusion that localises the penicillin-binding domain of penicillin-binding protein 3 of Escherichia coli

• Published in: FEBS letters 1984-10, Vol.176 (1), p.179-184
• Main Authors: Hedge, Philip J., Spratt, Brian G.
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - genetics; Bacterial Proteins - metabolism; beta-Galactosidase - genetics; Carboxypeptidases - genetics; Carrier Proteins - genetics; Carrier Proteins - metabolism; DNA Restriction Enzymes; DNA, Bacterial - metabolism; DNA, Recombinant - metabolism; Escherichia coli; Escherichia coli - genetics; Escherichia coli Proteins; Gene fusion; Hexosyltransferases; Muramoylpentapeptide Carboxypeptidase - genetics; Muramoylpentapeptide Carboxypeptidase - metabolism; Penicillin G - metabolism; Penicillin-binding protein; Penicillin-Binding Proteins; Penicillins - metabolism; Peptide Fragments - genetics; Peptide Fragments - metabolism; Peptidoglycan; Peptidoglycan Glycosyltransferase; Peptidyl Transferases; Transglycosylase-transpeptidase; β-Lactam antibiotic
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(84)80936-9

A gene fusion that links the COOH-terminal 349 amino acids of penicillin-binding protein 3 (60 kDa) of E.coli to the NH 2-terminus of β-galactosidase has been constructed. The fusion protein (38.5 kDa) retains the ability to bind benzylpenicillin with high affinity, establishing that the penicillin-binding domain (and presumably the penicillin-sensitive transpeptidase activity) of this high molecular mass penicillin-binding protein is located on a COOH-terminal functional domain.