Membrane-bound thiol-disulfide oxidoreductases in Bacillus subtilis

Detta är en avhandling från Lydur Erlendsson, Department of cell and organsimbiology, Sölvegatan 35, Lund

Författare: Lydur Erlendsson; Lunds Universitet.; Lund University.; [2003]

Nyckelord: MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; virologi; mykologi; Mikrobiologi; mycology; virology; bacteriology; Microbiology; sporulation; cytochrome c; thiol-disulfide oxidoreductases; Bacillus subtilis; membrane proteins; bakteriologi;

Sammanfattning: Disulfide bonds in proteins are found between cysteine residues and are usually important for either function or stability of proteins. Thiol-disulfide oxidoreductases catalyse the formation or breakage of disulfide bonds in proteins. The gram-positive endospore-forming bacterium Bacillus subtilis contains several membrane-bound thiol-disulfide oxidoreductases. BdbA, BdbB and CcdA have been described before. In this thesis BdbC, BdbD, ResA and StoA have been identified and studied. ·BdbD catalyses disulfide bond formation in proteins on the outer side of the cytoplasmic membrane and BdbC re-oxidises BdbD. ·BdbA and BdbB are apparent homologues of BdbD and BdbC, respectively. They appear to by specific for disulfide bond formation in the lanthionine Sublancin 168. ·ResA functions in cytochrome c synthesis. ·CcdA is involved in cytochrome c synthesis and endospore formation. ·StoA plays a role in endospore biogenesis.

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