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Characterization of endoplasmic reticulum oxidoreductase (ERO1) gene from Bombyx mori
- 언어ENG
- URLhttps://db.koreascholar.com/Article/Detail/290761
Disulfide bond formation, reduction and isomerization are important posttranslational modification in proteins that occur in most, if not all, living organisms. In eukatoyes, disulfide bond in substrate proteins are primarily formes by ERO1 and PDI. ERO1, oxidized by molecular oxygen, acts as a specific oxidant of PDI, which then makes disulfide bonds in folding proteins oxidized directly. It means that ERO1 plays an essential role in setting the redox potential in the ER, and the regulation of Ero1p activity is critical to maintain redox homeostasis and proper ER folding activity. We have isolated and analysed a endoplasmic reticulum oxidoreductase (ERO1) from Bombye mori. It apperas that both an N-terminal CxxxxC motif and a C-terminl CxxCxxC motif are necessary for Ero1p fuction. In vivo, the result of the 5day of 5th instar larvae by RT-PCR and Real-Time PCR shows that posterior silkgland, skin and mid silkgland are revealed more than rhose of other tissues. The same result for tissue distribution of transcripts is appeared about ERO1 and PDI. In Bombyx mori, ERO1 is also supposed to correlate with PDI. Afterwards, more experiments are needed to figure out accurate interrelation between ERO1 and PDI.
