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

Massimiliano Pagani, Stefania Pilati, Gloria Bertoli, Barbara Valsasina, Roberto Sitia

Research output: Contribution to journalArticle

35 Citations (Scopus)

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-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.

Original languageEnglish
Pages (from-to)117-120
Number of pages4
JournalFEBS Letters
Volume508
Issue number1
DOIs
Publication statusPublished - Nov 9 2001

Fingerprint

Yeast
Yeasts
Membranes
Endoplasmic Reticulum
Tail
Association reactions
Protein folding
Protein Folding
Protein Sorting Signals
Eukaryota
Lipids
Amino Acids
Growth

Keywords

  • Disulfide bond
  • Endoplasmic reticulum
  • Membrane insertion
  • Oxidative folding
  • Oxidoreductase
  • Redox
  • Secretion

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. / Pagani, Massimiliano; Pilati, Stefania; Bertoli, Gloria; Valsasina, Barbara; Sitia, Roberto.

In: FEBS Letters, Vol. 508, No. 1, 09.11.2001, p. 117-120.

Research output: Contribution to journalArticle

Pagani, Massimiliano ; Pilati, Stefania ; Bertoli, Gloria ; Valsasina, Barbara ; Sitia, Roberto. / The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. In: FEBS Letters. 2001 ; Vol. 508, No. 1. pp. 117-120.
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