Effect of protein disulfide isomerase on the rate-determining steps of the folding of bovine pancreatic ribonuclease A.

Abstract:

:The effects of protein disulfide isomerase (PDI) on the four structured des species that accumulate in the rate-determining steps of ribonuclease A folding were investigated at pH 8.0 and 15 degrees C. The results indicate that PDI catalyzes the conversion of the kinetically trapped intermediates, des-[26-84] and des-[58-110], by reshuffling them into the on-pathway intermediate, des-[40-95], and the formation of native protein, by acting as both a chaperone and an oxidase on this on-pathway intermediate. These results provide the first strong evidence for the mechanism of PDI in the rate-determining steps of the oxidative folding pathways of ribonuclease A. Our approach, using PDI and blocked PDI, combined with the fast-blocking 2-aminoethyl methanethiosulfonate method, may be generally applicable to the clarification of the effect of PDI on folding intermediates.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Shin HC,Song MC,Scheraga HA

doi

10.1016/s0014-5793(02)02825-9

keywords:

subject

Has Abstract

pub_date

2002-06-19 00:00:00

pages

77-80

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302028259

journal_volume

521

pub_type

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