Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding

Author:

Kadokura Hiroshi12,Tian Hongping12,Zander Thomas12,Bardwell James C. A.12,Beckwith Jon12

Affiliation:

1. Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.

2. Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

Abstract

DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed disulfide complexes between DsbA and its substrates. However, these complexes are difficult to detect, probably because of their short-lived nature. Here we show that it is possible to detect such covalent intermediates in vivo by a mutation in DsbA that alters cis proline-151. Further, this mutant allowed us to identify substrates of DsbA. Alteration of the cis proline, highly conserved among thioredoxin superfamily members, may be useful for the detection of substrates and intermediate complexes in other systems.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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