The C‐terminal domain of yeast Ero1p mediates membrane localization and is essential for function

FEBS Letters

Bertoli, Gloria¹  Pilati, Stefania¹  Valsasina, Barbara²  Pagani, Massimiliano¹  Sitia, Roberto¹ 

[1] Department of Molecular Pathology and Medicine, DiBiT-San Raffaele Scientific Institute, 20132 Milan, Italy;Biology Department, Pharmacia, 20014 Nerviano (MI), Italy

关键词: Disulfide bond;    Oxidative folding;    Oxidoreductase;    Redox;    Secretion;    Endoplasmic reticulum;    Membrane insertion;    ER;    endoplasmic reticulum;    PDI;    protein disulfide isomerase;   

DOI  :  10.1016/S0014-5793(01)03034-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown