Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 37, Pages 32705-32712Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.227181
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Funding
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) [19G0314, 19058008]
- Japan Society for the Promotion of Science
- Grants-in-Aid for Scientific Research [19GS0314, 19058008] Funding Source: KAKEN
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Oxidative protein folding in the endoplasmic reticulum is supported by efficient electron relays driven by enzymatic reactions centering on the ERO1-protein-disulfide isomerase (PDI) pathway. A controlled in vitro oxygen consumption assay was carried out to analyze the ERO1-PDI reaction. The results showed the pH-dependent oxidation of PDI by ERO1 alpha. Among several possible disulfide bonds regulating ERO1 alpha activity, Cys(94)-Cys(131) and Cys(99)-Cys(104) disulfide bonds are dominant regulators by excluding the involvement of the Cys(85)-Cys(391) disulfide in the regulation. The fine-tuned species specificity of the ERO1-PDI pathway was demonstrated by functional in vitro complementation assays using yeast and mammalian oxidoreductases. Finally, the results provide experimental evidence for the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1 alpha.
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