Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation

Proceedings of the National Academy of Sciences of the United States of America
Christopher L ColbertJohann Deisenhofer

Abstract

The covalent attachment of heme cofactors to the apo-polypeptides via thioether bonds is unique to the maturation of c-type cytochromes. A number of thiol-disulfide oxidoreductases prepare the apocytochrome for heme insertion in system I and II cytochrome c maturation. Although most thiol-disulfide oxidoreductases are nonspecific, the less common, specific thiol-disulfide oxidoreductases may be key to directing the usage of electrons. Here we demonstrate that unlike other thiol-disulfide oxidoreductases, the protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific for cytochrome c550 and utilizes alternate conformations to recognize redox partners. We report solution NMR evidence that ResA undergoes a redox-dependent conformational change between oxidation states, as well as data showing that ResA utilizes a surface cavity present only in the reduced state to recognize a peptide derived from cytochrome c550. Finally, we confirm that ResA is a specific thiol-disulfide oxidoreductase by comparing its reactivity to our mimetic peptide with its reactivity to oxidized glutathione, a nonspecific substrate. This study biochemically demonstrates the specificity of this thiol-disulfide oxidoreduc...Continue Reading

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Citations

Dec 21, 2006·Journal of the American Chemical Society·Norman MetanisPhilip E Dawson
Jul 16, 2010·The Journal of Biological Chemistry·Stéphane T GabillyPatrice P Hamel
May 6, 2011·The Journal of Biological Chemistry·Despoina A I MavridouChristina Redfield
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Sep 15, 2006·The Journal of Biological Chemistry·Allison LewinNick E Le Brun

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