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

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

Volume: 12 Issue: 1

Author(s): Ryoichi Tanaka, Makoto Mizukami and Masao Tokunaga

Affiliation:

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

Abstract: 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.

Cite this article as:

Tanaka Ryoichi, Mizukami Makoto and Tokunaga Masao, Novel Processing and Localization of catA, ccdA Associated Thiol-Disulfide Oxidoreductase, in Protein Hyper-Producing Bacterium Brevibacillus choshinensis, Protein & Peptide Letters 2005; 12 (1) . https://dx.doi.org/10.2174/0929866053406093