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PMID: 8654363 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.

The EMBO journal ·Vol. 15 ·No. 11 ·1996-06-03 ·Pages 2659-67

Chivers PT, Laboissière MC, Raines RT

Abstract

The rapid formation of native disulfide bonds in cellular proteins is necessary for the efficient use of cellular resources. This process is catalyzed in vitro by protein disulfide isomerase (PDI), with the PDI1 gene being essential for the viability of Saccharomyces cerevisiae. PDI is a member of the thioredoxin (Trx) family of proteins, which have the active-site motif CXXC. PDI contains two Trx domains as well as two domains unrelated to the Trx family. We find that the gene encoding Escherichia coli Trx is unable to complement PDI1 null mutants of S.cerevisiae. Yet, Trx can replace PDI if it is mutated to have a CXXC motif with a disulfide bond of high reduction potential and a thiol group of low pKa. Thus, an enzymic thiolate is both necessary and sufficient for the formation of native disulfide bonds in the cell.

MeSH Terms
Base Sequence Consensus Sequence DNA Primers/chemistry Disulfides/chemistry Escherichia coli/enzymology Isomerases/metabolism Molecular Sequence Data Oxidation-Reduction Protein Disulfide-Isomerases Protein Structure, Tertiary Proteins/chemistry Saccharomyces cerevisiae/enzymology Structure-Activity Relationship Thioredoxins/chemistry
Chemicals
DNA Primers Disulfides Proteins Thioredoxins Isomerases Protein Disulfide-Isomerases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Chivers P T
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706-1569, USA.
Laboissière M C
Raines R T
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1996-06-03
Pages
2659-67
Language
English
Region
England
NLM ID
8208664
PMCID
PMC450201
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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