ER-60 domains responsible for interaction with calnexin and calreticulin

Biochemistry
Reiko UradeYukino Arakaki

Abstract

ER-60 is a thiol oxidoreductase family protein of the endoplasmic reticulum that facilitates the oxidative folding of glycoproteins via interaction with calnexin (CNX) and calreticulin (CRT). In this study, we tried to identify the site of interaction with CNX and CRT in the ER-60 molecule. ER-60 was shown to be composed of at least four domains, named a, b, b', and a', by limited proteolysis. Recombinant fragments of ER-60, a, b', and a'c, were each expressed in Escherichia coli as an individual soluble folded protein that underwent a cooperative unfolding transition along a urea gradient. These fragments each gave the circular dichroism (CD) spectrum of the folded protein. On the other hand, fragment b, which did not undergo the cooperative unfolding transition along a urea gradient gel, did not show any sign of the folded structure on the CD measurement. However, subtraction of the spectra showed that the b domain was folded in wild-type ER-60 or abb'. Both a and a'c, which have a catalytic center CGHC motif, showed activity almost equivalent to half of that of wild-type ER-60. Extension from a or a'c to ab and abb' or b'a'c had little effect on their isomerase activity, suggesting that the b and b' domains hardly contribute...Continue Reading

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Citations

Sep 22, 2006·Antioxidants & Redox Signaling·Agnes GörlachThomas Kietzmann
Aug 26, 2014·Applied Biochemistry and Biotechnology·Mohammad Aasif DarFaizan Ahmad
Jun 27, 2007·Biochemical and Biophysical Research Communications·Shinya HagiharaYukishige Ito
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Jun 28, 2005·The FEBS Journal·Shinya KamauchiReiko Urade
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Jan 24, 2006·Journal of Biochemistry·Hirokazu OkudoReiko Urade
Dec 30, 2004·The Journal of Biological Chemistry·Johannes HaugstetterLars Ellgaard
Feb 5, 2019·Bioscience, Biotechnology, and Biochemistry·Reiko Urade
Jun 3, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Yuya TanikawaMasaki Okumura

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