Abstract
Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of disulfide bonds in secretory proteins. Here we report the cloning and characterization of a mammalian gene (ERO1-L) that shares extensive homology with the Saccharomyces cerevisiae ERO1 gene, required in yeast for oxidative protein folding. When expressed in mammalian cells, the product of the human ERO1-L gene colocalizes with ER markers and displays Endo-H-sensitive glycans. In isolated microsomes, ERO1-L behaves as a type II integral membrane protein. ERO1-L is able to complement several phenotypic traits of the yeast thermosensitive mutant ero1-1, including temperature and dithiothreitol sensitivity, and intrachain disulfide bond formation in carboxypeptidase Y. ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. These results strongly suggest that ERO1-L is involved in oxidative ER protein folding in mammalian cells.
| Original language | English |
|---|---|
| Pages (from-to) | 4827-4833 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 275 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Feb 18 2000 |
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ASJC Scopus subject areas
- Biochemistry
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ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. / Cabibbo, Andrea; Pagani, Massimiliano; Fabbri, Marco; Rocchi, Mariano; Farmery, Mark R.; Bulleid, Neil J.; Sitia, Roberto.
In: Journal of Biological Chemistry, Vol. 275, No. 7, 18.02.2000, p. 4827-4833.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
AU - Cabibbo, Andrea
AU - Pagani, Massimiliano
AU - Fabbri, Marco
AU - Rocchi, Mariano
AU - Farmery, Mark R.
AU - Bulleid, Neil J.
AU - Sitia, Roberto
PY - 2000/2/18
Y1 - 2000/2/18
N2 - Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of disulfide bonds in secretory proteins. Here we report the cloning and characterization of a mammalian gene (ERO1-L) that shares extensive homology with the Saccharomyces cerevisiae ERO1 gene, required in yeast for oxidative protein folding. When expressed in mammalian cells, the product of the human ERO1-L gene colocalizes with ER markers and displays Endo-H-sensitive glycans. In isolated microsomes, ERO1-L behaves as a type II integral membrane protein. ERO1-L is able to complement several phenotypic traits of the yeast thermosensitive mutant ero1-1, including temperature and dithiothreitol sensitivity, and intrachain disulfide bond formation in carboxypeptidase Y. ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. These results strongly suggest that ERO1-L is involved in oxidative ER protein folding in mammalian cells.
AB - Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of disulfide bonds in secretory proteins. Here we report the cloning and characterization of a mammalian gene (ERO1-L) that shares extensive homology with the Saccharomyces cerevisiae ERO1 gene, required in yeast for oxidative protein folding. When expressed in mammalian cells, the product of the human ERO1-L gene colocalizes with ER markers and displays Endo-H-sensitive glycans. In isolated microsomes, ERO1-L behaves as a type II integral membrane protein. ERO1-L is able to complement several phenotypic traits of the yeast thermosensitive mutant ero1-1, including temperature and dithiothreitol sensitivity, and intrachain disulfide bond formation in carboxypeptidase Y. ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. These results strongly suggest that ERO1-L is involved in oxidative ER protein folding in mammalian cells.
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UR - http://www.scopus.com/inward/citedby.url?scp=0034681340&partnerID=8YFLogxK
U2 - 10.1074/jbc.275.7.4827
DO - 10.1074/jbc.275.7.4827
M3 - Article
C2 - 10671517
AN - SCOPUS:0034681340
VL - 275
SP - 4827
EP - 4833
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 7
ER -