DOI QR코드

DOI QR Code

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

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.

Keywords

References

  1. Baker KM, Chakravarthi S, Langton KP, Sheppard AM, Lu H, Bulleid NJ (2008) Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. EMBO J 27, 2988-2997. https://doi.org/10.1038/emboj.2008.230
  2. Dias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, et al. (2005) Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta. J Biol Chem 280, 33066-33075. https://doi.org/10.1074/jbc.M505023200
  3. Frand AR, Kaiser CA (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1, 161-170. https://doi.org/10.1016/S1097-2765(00)80017-9
  4. Frand AR, Kaiser CA (1999) ERO1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4, 469-477. https://doi.org/10.1016/S1097-2765(00)80198-7
  5. Goo TW, Yun EY, Kim SW, Choi KH, Kang SW, Shin KS, et al. (2008) Domain a' of Bombyx mori protein disulfide isomerase has chaperone activity. Z Naturforsch C 63(5-6):435-9. https://doi.org/10.1515/znc-2008-5-620
  6. Harding HP, Zhang Y, Zeng H, Novoa I, Lu PD, Calfon M, et al. (2003) An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11, 619-633. https://doi.org/10.1016/S1097-2765(03)00105-9
  7. Hoog C (1991) Isolation of a large number of novel mammalian genes by a differential cDNA libraryn screening strategy. Nucleic Acids Res 19, 6123-6127. https://doi.org/10.1093/nar/19.22.6123
  8. Jessop CE, Chakravarthi S, Watkins RH, Bulleid NJ (2004) Oxidative protein folding in the mammalianendoplasmic reticulum. Biochem Soc Trans 32, 655-658. https://doi.org/10.1042/BST0320655
  9. Lyles MM, Gilbert HF (1991) Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry 30, 619-625. https://doi.org/10.1021/bi00217a005
  10. Pollard MG, Travers KJ, Weissman JS (1998) ERO1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 171-182.
  11. Schroder M (2008) Engineering eukaryotic protein factories. Biotechnol Lett 30, 187-196. https://doi.org/10.1007/s10529-007-9524-1
  12. Seo M, Ryou HJ, Yun EY, Goo TW (2015) Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori. Int J Mol Sci,16(11), 26520-26529. https://doi.org/10.3390/ijms161125977
  13. Sevier CS, Kaiser CA (2002) Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol 3, 836-847.
  14. Sevier CS, Kaiser CA (2006) Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1. Mol Biol Cell 17, 2256-2266. https://doi.org/10.1091/mbc.e05-05-0417
  15. Tu BP, Weissman JS (2002) The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol Cell 10, 983-994. https://doi.org/10.1016/S1097-2765(02)00696-2
  16. Tu BP, Weissman JS (2004) Oxidative protein folding in eukaryotes: Mechanisms and consequences. J Cell Biol, 164, 341-346. https://doi.org/10.1083/jcb.200311055
  17. Xiao R, Solovyov A, Gilbert HF, Holmgren A, Lundstrom-Ljung J (2001) Combinations of proteindisulfide isomerase domains show that there is little correlation between isomerase activity and wildtype growth. J Biol Chem 276, 27975-27980. https://doi.org/10.1074/jbc.M104203200
  18. Zito E (2015) ERO1: A protein disulfide oxidase and H2O2 producer. Free Radic Biol Med 83, 299-304. https://doi.org/10.1016/j.freeradbiomed.2015.01.011
  19. Zito E, Chin KT, Blais J, Harding HP, Ron D (2010a) ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis. J Cell Biol 188, 821-832. https://doi.org/10.1083/jcb.200911086
  20. Zito E, Melo EP, Yang Y, Wahlander A, Neubert TA, Ron D (2010b) Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol Cell 40, 787-797 https://doi.org/10.1016/j.molcel.2010.11.010