Oxidative Protein Folding: Many Different Ways to Introduce Disulfide Bonds

摘要

A DISULFIDE BOND IS A COVALENT LINKAGE between two cysteines. Formation of disulfide bonds contributes to the stability, activity, and folding of many proteins. In the 1960s, Anfinsen and his coworkers showed that the formation of disulfide bonds can occur spontaneously in vitro in the presence of O_2 (1), which led to the long-held conviction that disulfide bond formation was a spontaneous process in vivo. It was 30 years later that discovery of mutations in the gene dsbA of Escherichia coli revealed that disulfide bond formation is a catalyzed process in vivo (2, 6). Later, increasingly, enzymes are being identified that promote the oxidative folding of proteins. Half of the articles in this forum issue highlight the mechanisms employed by various organisms to introduce disulfide bonds into proteins. A surprising variety of mechanisms and protein structures are evolved to catalyze oxidative protein folding which takes place at unexpectedly diverse cellular locations