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

doi:10.1016/S0014-5793(01)03034-4

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

IRCCS Ospedale San Raffaele

Research output: Contribution to journal › Article › peer-review

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	https://doi.org/10.1016/S0014-5793(01)03034-4
Publication status	Published - Nov 9 2001

Keywords

Disulfide bond
Endoplasmic reticulum
Membrane insertion
Oxidative folding
Oxidoreductase
Redox
Secretion

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

Access to Document

10.1016/S0014-5793(01)03034-4

Fingerprint Dive into the research topics of 'The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function'. Together they form a unique fingerprint.

Cite this

@article{27f0d729a682444a91e6ddca6bf84ad8,

title = "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-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.",

keywords = "Disulfide bond, Endoplasmic reticulum, Membrane insertion, Oxidative folding, Oxidoreductase, Redox, Secretion",

author = "Massimiliano Pagani and Stefania Pilati and Gloria Bertoli and Barbara Valsasina and Roberto Sitia",

year = "2001",

month = nov,

day = "9",

doi = "10.1016/S0014-5793(01)03034-4",

language = "English",

volume = "508",

pages = "117--120",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1",

}

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

C2 - 11707280

AN - SCOPUS:0035834372

VL - 508

SP - 117

EP - 120

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -