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 language | English |
|---|---|
| Pages (from-to) | 117-120 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 508 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Nov 9 2001 |
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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 journal › Article
}
TY - JOUR
T1 - The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function
AU - Pagani, Massimiliano
AU - Pilati, Stefania
AU - Bertoli, Gloria
AU - Valsasina, Barbara
AU - Sitia, Roberto
PY - 2001/11/9
Y1 - 2001/11/9
N2 - 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.
AB - 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.
KW - Disulfide bond
KW - Endoplasmic reticulum
KW - Membrane insertion
KW - Oxidative folding
KW - Oxidoreductase
KW - Redox
KW - Secretion
UR - http://www.scopus.com/inward/record.url?scp=0035834372&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035834372&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(01)03034-4
DO - 10.1016/S0014-5793(01)03034-4
M3 - Article
VL - 508
SP - 117
EP - 120
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -