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Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin

Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin The formation of disulphide bonds is essential to the structure and function of proteins. These bonds rapidly form either co-translationally or immediately post-translationally in the lumen of the endoplasmic reticulum1,2. Native disulphide pairing for such proteins has been achieved in vitro; however, the rates of reassembly are slow and the conditions non-physiological3,4. To account for these observations, Anfinsen et al. proposed that a ‘disulphide interchange protein’ was the in vivo catalyst of disulphide bond rearrangement5. Other groups discovered an activity with similar characteristics that catalysed the reductive cleavage of insulin and may be associated with insulin degradation6,7, although this result has been disputed8. The enzyme involved, protein disulphide isomerase (PDI; EC 5.3.4.1), may be the in vivo catalyst of disulphide bond formation9. Here we describe the sequence of cloned rat liver PDI complementary DNA which predicts a protein with two distinct regions homologous with Escherichia coli thioredoxin, a known cofactor in oxidation–reduction reactions10. Each of these regions contains the presumed active site sequence Trp-Cys-Gly-His-Cys-Lys, suggesting that PDI, similar in action to thioredoxin, catalyses disulphide bond interchange via an internal disulphide–sulphydryl interchange. The cDNA predicts a signal peptide consistent with the view that PDI is a luminal endoplasmic reticulum protein. PDI messenger RNA, although ubiquitous, is more highly concentrated in secretory cells. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin

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References (41)

Publisher
Springer Journals
Copyright
Copyright © 1985 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/317267a0
Publisher site
See Article on Publisher Site

Abstract

The formation of disulphide bonds is essential to the structure and function of proteins. These bonds rapidly form either co-translationally or immediately post-translationally in the lumen of the endoplasmic reticulum1,2. Native disulphide pairing for such proteins has been achieved in vitro; however, the rates of reassembly are slow and the conditions non-physiological3,4. To account for these observations, Anfinsen et al. proposed that a ‘disulphide interchange protein’ was the in vivo catalyst of disulphide bond rearrangement5. Other groups discovered an activity with similar characteristics that catalysed the reductive cleavage of insulin and may be associated with insulin degradation6,7, although this result has been disputed8. The enzyme involved, protein disulphide isomerase (PDI; EC 5.3.4.1), may be the in vivo catalyst of disulphide bond formation9. Here we describe the sequence of cloned rat liver PDI complementary DNA which predicts a protein with two distinct regions homologous with Escherichia coli thioredoxin, a known cofactor in oxidation–reduction reactions10. Each of these regions contains the presumed active site sequence Trp-Cys-Gly-His-Cys-Lys, suggesting that PDI, similar in action to thioredoxin, catalyses disulphide bond interchange via an internal disulphide–sulphydryl interchange. The cDNA predicts a signal peptide consistent with the view that PDI is a luminal endoplasmic reticulum protein. PDI messenger RNA, although ubiquitous, is more highly concentrated in secretory cells.

Journal

Nature – Springer Journals

Published: Sep 19, 1985

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