International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Enzymatic activity of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori

  • Park, Kwanho (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Yun, Eun-Young (Graduate School of Integrated Bioindustry, Sejong University) ;
  • Goo, Tae-Won (Department of Biochemistry, School of Medicine, Dongguk University)
  • Received : 2018.06.20
  • Accepted : 2018.09.11
  • Published : 2018.09.30
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Abstract

Most proteins produced in the endoplasmic reticulum (ER) of eukaryotic cells fold via disulfide formation (oxidative folding). Oxidative folding is catalyzed by protein disulfide isomerase (PDI) and PDI-related ER protein thiol disulfide oxidoreductases (ER oxidoreductases). In yeast and mammals, ER oxidoreductin-1s (ERO1s) supply oxidizing equivalent to the active centers of PDI. We previously identified and characterized the ERO1 of Bombyx mori (bERO1) as a thioredoxin-like protein that shares primary sequence homology with other ERO1s. Here we compare the reactivation of inactivated rRNase and sRNase by bERO1, and show that bERO1 and bPDI cooperatively refold denatured RNase A. This is the first result suggesting that bERO1 plays an essential role in ER quality control through the combined activities of bERO1 and bPDI as a catalyst of protein folding in the ER and sustaining cellular redox homeostasis.

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References

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