Abstract
To understand better the role of non-clathrin coat proteins in membrane traffic, we have cloned and characterized two essential genes encoding subunits of the yeast coatomer, SEC26 and SEC27. Sec26p is a 109-kDa protein that shares 43% sequence identity with mammalian β-coat protein (β-COP). Sec26p-depleted cells accumulate endoplasmic reticulum (ER) forms of secretory precursor proteins, and growth ceases after a dramatic accumulation of ER membranes. Sec26p overproduction partially suppresses sec27-1, a new mutant that shows a temperature-sensitive defect in ER-to-Golgi transport. The SEC27 gene was cloned, and the sequence predicts a 99.4-kDa protein with 45% sequence identity to mammalian β'-COP. Our sequence data support a two- domain model for the SEC27 protein: a conserved amino-terminal domain, composed of five WD-40 repeats similar to those found in β-subunits of trimeric G proteins, and a less conserved carboxyl-terminal domain. Genetic interactions connect sec27-1 and sec21-1 (coatomer γ subunit) with the ARF1 and ARF2 genes and with the SEC22, BET1, and BOS1 genes, which encode membrane proteins involved in ER-to-Golgi transport.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 24486-24495 |
| Number of pages | 10 |
| Journal | Journal of Biological Chemistry |
| Volume | 269 |
| Issue number | 39 |
| State | Published - Jan 1 1994 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Yeast β- and β'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic. / Duden, R.; Hosobuchi, M.; Hamamoto, S.; Winey, Mark; Byers, B.; Schekman, R.
In: Journal of Biological Chemistry, Vol. 269, No. 39, 01.01.1994, p. 24486-24495.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Yeast β- and β'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic
AU - Duden, R.
AU - Hosobuchi, M.
AU - Hamamoto, S.
AU - Winey, Mark
AU - Byers, B.
AU - Schekman, R.
PY - 1994/1/1
Y1 - 1994/1/1
N2 - To understand better the role of non-clathrin coat proteins in membrane traffic, we have cloned and characterized two essential genes encoding subunits of the yeast coatomer, SEC26 and SEC27. Sec26p is a 109-kDa protein that shares 43% sequence identity with mammalian β-coat protein (β-COP). Sec26p-depleted cells accumulate endoplasmic reticulum (ER) forms of secretory precursor proteins, and growth ceases after a dramatic accumulation of ER membranes. Sec26p overproduction partially suppresses sec27-1, a new mutant that shows a temperature-sensitive defect in ER-to-Golgi transport. The SEC27 gene was cloned, and the sequence predicts a 99.4-kDa protein with 45% sequence identity to mammalian β'-COP. Our sequence data support a two- domain model for the SEC27 protein: a conserved amino-terminal domain, composed of five WD-40 repeats similar to those found in β-subunits of trimeric G proteins, and a less conserved carboxyl-terminal domain. Genetic interactions connect sec27-1 and sec21-1 (coatomer γ subunit) with the ARF1 and ARF2 genes and with the SEC22, BET1, and BOS1 genes, which encode membrane proteins involved in ER-to-Golgi transport.
AB - To understand better the role of non-clathrin coat proteins in membrane traffic, we have cloned and characterized two essential genes encoding subunits of the yeast coatomer, SEC26 and SEC27. Sec26p is a 109-kDa protein that shares 43% sequence identity with mammalian β-coat protein (β-COP). Sec26p-depleted cells accumulate endoplasmic reticulum (ER) forms of secretory precursor proteins, and growth ceases after a dramatic accumulation of ER membranes. Sec26p overproduction partially suppresses sec27-1, a new mutant that shows a temperature-sensitive defect in ER-to-Golgi transport. The SEC27 gene was cloned, and the sequence predicts a 99.4-kDa protein with 45% sequence identity to mammalian β'-COP. Our sequence data support a two- domain model for the SEC27 protein: a conserved amino-terminal domain, composed of five WD-40 repeats similar to those found in β-subunits of trimeric G proteins, and a less conserved carboxyl-terminal domain. Genetic interactions connect sec27-1 and sec21-1 (coatomer γ subunit) with the ARF1 and ARF2 genes and with the SEC22, BET1, and BOS1 genes, which encode membrane proteins involved in ER-to-Golgi transport.
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UR - http://www.scopus.com/inward/citedby.url?scp=0028170420&partnerID=8YFLogxK
M3 - Article
C2 - 7929113
AN - SCOPUS:0028170420
VL - 269
SP - 24486
EP - 24495
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 39
ER -