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

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 Lett

journal_title

FEBS letters

authors

Pagani M,Pilati S,Bertoli G,Valsasina B,Sitia R

doi

10.1016/s0014-5793(01)03034-4

keywords:

subject

Has Abstract

pub_date

2001-11-09 00:00:00

pages

117-20

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)03034-4

journal_volume

508

pub_type

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