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Novel Processing and Localization of catA, ccdA Associated Thiol-Disulfide Oxidoreductase, in Protein Hyper-Producing Bacterium Brevibacillus choshinensis

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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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Keywords: brevibacillus choshinensis; cata; ccda; localization; processing; thiol-disulfide oxidoreductase

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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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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