The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds

Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active site CGHC. Haploid pdi1 delta Saccharomyces cerevisiae are inviable, but can be complemented with either a wild-type...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-11, Vol.270 (47), p.28006-28009
Main Authors: Laboissiere, M.C.A. (University of Wisconsin, Madison, WI.), Sturley, S.L, Raines, R.T
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Cloning, Molecular
Disulfides - metabolism
Endoplasmic Reticulum - enzymology
Escherichia coli
GENE
GENES
Genetic Complementation Test
GENETICA
GENETIQUE
Haploidy
ISOMERASAS
ISOMERASE
Isomerases - biosynthesis
Isomerases - genetics
Isomerases - metabolism
ISOMERISATION
ISOMERIZACION
Kinetics
Molecular Sequence Data
MUTACION INDUCIDA
Mutagenesis, Site-Directed
MUTANT
MUTANTES
MUTATION PROVOQUEE
Oligodeoxyribonucleotides
OXIDACION
Oxidation-Reduction
OXYDATION
Protein Disulfide-Isomerases
RAT
RATA
Rats
REDUCCION
REDUCTION
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Serine
Stereoisomerism
TRANSFORMACION GENETICA
TRANSFORMATION GENETIQUE
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Summary:Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active site CGHC. Haploid pdi1 delta Saccharomyces cerevisiae are inviable, but can be complemented with either a wild-type rat PDI gene or a mutant gene coding for CGHS PDI (shufflease). In contrast, pdi1 delta yeast cannot be complemented with a gene coding for SGHC PDI. In vitro, shufflease is an efficient catalyst for the isomerization of existing disulfide bonds but not for dithiol oxidation or disulfide bond reduction. SGHC PDI catalyzes none of these processes. These results indicate that in vivo protein folding pathways contain intermediates with non-native disulfide bonds, and that the essential role of PDI is to unscramble these intermediates
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.47.28006