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

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

Journal Name: Protein & Peptide Letters

Volume 12 , Issue 1 , 2005

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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

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Article Details

VOLUME: 12
ISSUE: 1
Year: 2005
Page: [95 - 98]
Pages: 4
DOI: 10.2174/0929866053406093

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