Journal
FEBS LETTERS
Volume 508, Issue 1, Pages 117-120Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)03034-4
Keywords
disulfide bond; oxidative folding; oxidoreductase; redox; secretion; endoplasmic reticulum; membrane insertion
Funding
- Telethon [GP0117Y01] Funding Source: Medline
Ask authors/readers for more resources
In eukaryotes, members of the Ero1 family control oxidative protein folding in the endoplasmic reticulum (ER). Yeast Ero1p is tightly associated with the ER membrane, despite cleavage of the leader peptide, the only hydrophobic sequence that could mediate lipid insertion. In contrast, human Ero1-L alpha and a yeast mutant (Ero1p DeltaC) lacking the 127 C-terminal amino acids are soluble when expressed in yeast. Neither Ero1-L alpha nor Ero1p DeltaC complements an ERO1 disrupted strain. Appending the yeast C-terminal tail to human Ero1-L alpha restores membrane association and allows growth of ERO1 disrupted cells. Therefore, the tail of Ero1p mediates membrane association and is crucial for function. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available