Chemistry Letters
Online ISSN : 1348-0715
Print ISSN : 0366-7022
ISSN-L : 0366-7022
Reshuffling Activity of Protein Disulfide Isomerase Reduces Refolding Yield in the Structure-forming Step of the Oxidative Protein Folding Reaction
Rituraj PalVeronica GonzalezMahesh Narayan
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2010 Volume 39 Issue 3 Pages 263-265


We have determined the impact of the oxidoreductase chaperone protein disulfide isomerase (PDI) on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins. This is achieved by using a novel tool to trap and populate native-disulfide-containing intermediates in unstructured forms that are poised to fold. Our data reveals that PDI inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone. Such an anomalous behavior of PDI during a key step in oxidative regeneration may contribute to misfolding in the endoplasmic reticulum, aggregation, and neurodegenerative disease.

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© 2010 The Chemical Society of Japan
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