Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori

International Journal of Molecular Sciences

Minchul Seo¹  Hee-Joo Ryou²  Eun-Young Yun²  Tae-Won Goo³ 

[1] Institute of Medical Research, Dongguk University College of Medicine, Gyeongju 38067, Korea;Department of Agricultural Biology, National Academy of Agricultural Science, RDA, Wanju-gun 55365, Korea;;Department of Biochemistry, Dongguk University College of Medicine, Gyeongju 38067, Korea

关键词: Bombyx mori;    endoplasmic reticulum oxidoreductin 1 (ERO1);    protein disulfide isomerase (PDI);    disulfide bond;   

DOI  :  10.3390/ijms161125977

来源: mdpi

【 摘 要 】

We isolated a complementary DNA (cDNA) clone encoding endoplasmic reticulum oxidoreductin 1 (bERO1, a specific oxidant of protein disulfide isomerase (PDI)) from Bombyx mori. This protein has a putative open reading frame (ORF) of 489 amino acids and a predicted size of 57.4 kDa. Although bERO1 protein shares less than 57% amino acid sequence homology with other reported ERO1s, it contains two conserved redox active motifs, a Cys-X-X-X-X-Cys motif of N-terminal and Cys-X-X-Cys-X-X-Cys motif of C-terminal. Both motifs are typically present in ERO1 protein family members. The bEro1 mRNA expression was highest in posterior silk gland on the sixth day of the 5th instar larvae. Expression of bEro1 mRNA also markedly increased during endoplasmic reticulum (ER) stress induced by stimulation with antimycin, calcium ionophore A23187, dithiothreitol, H₂O₂, monencin, and tunicamycin. In addition, expression levels of bEro1 exactly coincided with that of bPdi. 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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.