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J. Bacteriol., Jul 1996, 4306-4309, Vol 178, No. 14
Copyright © 1996, American Society for Microbiology

Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA

LE Elksne and BA Rasmussen
Discovery Research, Wyeth-Ayerst Research, Pearl River, New York 10965,USA.

It has previously been shown that functional expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli requires a mutation in either dsbA or dsbB, components of a periplasmic disulfide bond-catalyzing system. Site-directed mutagenesis resulting in the substitution of various amino acids for two of the three cysteine residues within CcrA allowed the expression of CcrA in a dsb+ background. This finding supports the hypothesis that DsbA creates aberrant disulfide bonds involving the Cys residues of CcrA.


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