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

Cited 0 time in scopus
Metadata Downloads
Domain a′ of Bombyx mori protein disulfide isomerase has chaperone activity
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
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.
Bombyx moriPDI activityProtein disulfide isomerase (PDI)
Walter De Gruyter Gmbh
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Ochang Branch Institute > Division of National Bio-Infrastructure > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.