Domain a′ of Bombyx mori protein disulfide isomerase has chaperone activity

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Title
Domain a′ of Bombyx mori protein disulfide isomerase has chaperone activity
Author(s)
T W Goo; E Y Yun; S W Kim; K H Choi; S W Kang; Kee Sun ShinKweon Yu; O Y Kwon
Bibliographic Citation
Zeitschrift fur Naturforschung Section C-A Journal of Biosciences, vol. 63, no. 5, pp. 435-439
Publication Year
2008
Abstract
Protein disulfide isomerase (PDI) is an endoplasmic reticulum (ER)-localized multifunctional enzyme that can function as a disulfide oxidase, a reductase, an isomerase, and a chaperone. The domain organization of PDI is abb′xa′c, with two catalytic (CxxC) motifs and a KDEL ER retention motif. The members of the PDI family exhibit differences in tissue distribution, specificity, and intracellular localization. We previously identified and characterized the PDI of Bombyx mori (bPDI) as a thioredoxin-like protein that shares primary sequence homology with other PDIs. Here we compare the reactivation of inactivated rRNase and sRNase by bPDI and three bPDI mutants, and show that bPDI has mammalian PDI-like activity. On its own, the N-terminal a domain does not retain this activity, but the a′ domain does. This is the first report of chaperone activity only in the a′ domain, but not in the a domain.
Keyword
Bombyx moriPDI activityProtein disulfide isomerase (PDI)
ISSN
0939-5075
Publisher
Walter De Gruyter Gmbh
DOI
http://dx.doi.org/10.1515/znc-2008-5-620
Type
Article
Appears in Collections:
Division of Biomaterials Research > Industrial Bio-materials Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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