Title: Identification of a protein required for disulfide bond formation in vivo
Abstract: <h2>Abstract</h2> We describe a mutation (<i>dsbA</i>) that renders Escherichia coli severely defective in disulfide bond formation. In <i>dsbA</i> mutant cells, pulse-labeled β-lactamase, alkaline phosphatase, and OmpA are secreted but largely lack disulfide bonds. These disulfideless proteins may represent in vivo folding intermediates, since they are protease sensitive and chase slowly into stable oxidized forms. The <i>dsbA</i> gene codes for a 21,000 M<sub>r</sub> periplasmic protein containing the sequence cys-pro-his-cys, which resembles the active sites of certain disulfide oxidoreductases. The purified DsbA protein is capable of reducing the disulfide bonds of insulin, an activity that it shares with these disulfide oxidoreductases. Our results suggest that disulfide bond formation is facilitated by DsbA in vivo.
Publication Year: 1991
Publication Date: 1991-11-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 957
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