Winter, Jeannette and Gleiter, Stefan and Klappa, Peter and Lilie, Hauke (2011) Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity. Protein Science, 20 (3). pp. 588-596. ISSN 0961-8368 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
Protein disulfide isomerase (PDI) supports proinsulin folding as chaperone and isomerase. Here, we focus on how the two PDI functions influence individual steps in the complex folding process of proinsulin. We generated a PDI mutant (PDI-aba′c) where the b′ domain was partially deleted, thus abolishing peptide binding but maintaining a PDI-like redox potential. PDI-aba′c catalyzes the folding of human proinsulin by increasing the rate of formation and the final yield of native proinsulin. Importantly, PDI-aba′c isomerizes non-native disulfide bonds in completely oxidized folding intermediates, thereby accelerating the formation of native disulfide bonds. We conclude that peptide binding to PDI is not essential for disulfide isomerization in fully oxidized proinsulin folding intermediates.
|Uncontrolled keywords:||oxidative protein folding;disulfide bond formation;chaperone;disulfide isomerization;folding intermediate|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||08 Oct 2012 13:40|
|Last Modified:||30 Jan 2013 12:48|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/31384 (The current URI for this page, for reference purposes)|