Novel Processing and Localization of catA, ccdA Associated Thiol-Disulfide Oxidoreductase, in Protein Hyper-Producing Bacterium Brevibacillus choshinensis
Previously, we have cloned ccdA and its associated thiol-disulfide oxidoreductase gene, catA, in Brevibacillus choshinensis. CcdA is known to be an integral membrane protein and its associated oxidoreductase homologues are believed to be membrane anchoring proteins, both providing reducing equivalents across the membrane to control correct disulfide bond formation. Here, we found that CatA is first localized as a membrane bound form and then slowly released into the cellular periphery and culture medium with cleavage at a novel processing site.
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Document Type: Review Article
Affiliations: Faculty of Agriculture,Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
Publication date: 2005-01-01
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