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.
Tanaka
Ryoichi
R
Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
Mizukami
Makoto
M
Tokunaga
Masao
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002374:Catalase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000201:enzymology*; D008565:Membrane Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D011490:Protein Disulfide Reductase (Glutathione) / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; C068355:CcdA protein, Bacteria; D008565:Membrane Proteins; D002374:Catalase; D011490:Protein Disulfide Reductase (Glutathione)