Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx mori.
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.
['Seo|Minchul|M|', 'Ryou|Hee-Joo|HJ|', 'Yun|Eun-Young|EY|', 'Goo|Tae-Won|TW|']
D020816:Amino Acid Motifs D000595:Amino Acid Sequence D000818:Animals D001483:Base Sequence D012831:Bombyx D018076:DNA, Complementary D004721:Endoplasmic Reticulum D059865:Endoplasmic Reticulum Stress D015870:Gene Expression D008969:Molecular Sequence Data D009928:Organ Specificity D019704:Protein Disulfide-Isomerases D054730:Protein Interaction Domains and Motifs
Bombyx mori protein disulfide isomerase (PDI) disulfide bond endoplasmic reticulum oxidoreductin 1 (ERO1)