Mutational analysis of the oxidoreductase ERp57 reveals the importance of the two central residues in the redox motif.

SM Beynon-Jones, AN Antoniou, Simon John Powis

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

The oxidoreductase ERp57 is involved in the formation and breaking of disulfide bonds in assembling proteins within the environment of the endoplasmic reticulum. Site-directed mutants of the redox-active Cys-GIy-His-Cys motif within an isolated ERp57 sub-domain have been studied. Whereas mutation of either cysteine residue abolished reductase activity, substitution of the central residues resulted in retention of partial activity. Alkylation studies indicated that the central residue mutants retained the normal disulfide bond in the motif, whereas this disulfide bond became more resistant to reduction following addition of a third residue into the redox motif, demonstrating an optimum spacing within the redox-active motif of ERp57. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)1897-1902
Number of pages6
JournalFEBS Letters
Volume580
DOIs
Publication statusPublished - 20 Mar 2006

Keywords

  • ERp57
  • oxidoreductase
  • PROTEIN DISULFIDE-ISOMERASE
  • THIOL-DEPENDENT REDUCTASE
  • PEPTIDE-LOADING COMPLEX
  • THIOREDOXIN-LIKE DOMAIN
  • ACTIVE-SITE CYSTEINE
  • CLASS-I MOLECULES
  • ENDOPLASMIC-RETICULUM
  • IDENTIFICATION
  • FAMILY
  • FORM

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