Abstract:
: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-Lalpha and a yeast mutant (Ero1pDeltaC) lacking the 127 C-terminal amino acids are soluble when expressed in yeast. Neither Ero1-Lalpha nor Ero1pDeltaC complements an ERO1 disrupted strain. Appending the yeast C-terminal tail to human Ero1-Lalpha restores membrane association and allows growth of ERO1 disrupted cells. Therefore, the tail of Ero1p mediates membrane association and is crucial for function.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pagani M,Pilati S,Bertoli G,Valsasina B,Sitia Rdoi
10.1016/s0014-5793(01)03034-4keywords:
subject
Has Abstractpub_date
2001-11-09 00:00:00pages
117-20issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(01)03034-4journal_volume
508pub_type
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