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

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...

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Bibliographic Details
Published in:Journal of bacteriology 1996, Vol.178 (14), p.4306-4309
Main Authors: Alksne, LE, Rasmussen, BA
Format: Article
Language:English
Subjects:
Bacteroides fragilis
Escherichia coli
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Summary: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 super(+) background. This finding supports the hypothesis that DsbA creates aberrant disulfide bonds involving the Cys residues of CcrA.
ISSN:0021-9193
DOI:10.1128/jb.178.14.4306-4309.1996