Premium
The C‐terminal domain of yeast Ero1p mediates membrane localization and is essential for function
Author(s) -
Pagani Massimiliano,
Pilati Stefania,
Bertoli Gloria,
Valsasina Barbara,
Sitia Roberto
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03034-4
Subject(s) - endoplasmic reticulum , yeast , saccharomyces cerevisiae , biology , mutant , membrane , microbiology and biotechnology , biochemistry , function (biology) , gene
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‐Lα and a yeast mutant (Ero1pΔC) lacking the 127 C‐terminal amino acids are soluble when expressed in yeast. Neither Ero1‐Lα nor Ero1pΔC complements an ERO1 disrupted strain. Appending the yeast C‐terminal tail to human Ero1‐Lα restores membrane association and allows growth of ERO1 disrupted cells. Therefore, the tail of Ero1p mediates membrane association and is crucial for function.