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.
Keywords: brevibacillus choshinensis, ccda, cata, thiol-disulfide oxidoreductase, localization, processing
Protein & Peptide Letters
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.
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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
DOI https://dx.doi.org/10.2174/0929866053406093 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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