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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
39
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pubmed:dateCreated |
1994-10-27
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pubmed:databankReference | |
pubmed:abstractText |
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 beta-coat protein (beta-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 beta'-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 beta-subunits of trimeric G proteins, and a less conserved carboxyl-terminal domain. Genetic interactions connect sec27-1 and sec21-1 (coatomer gamma 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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
269
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pubmed:geneSymbol |
ARF1,
ARF2,
BET1,
BOS1,
SEC26,
SEC27,
sec21-1,
sec27-1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24486-95
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7929113-Amino Acid Sequence,
pubmed-meshheading:7929113-Animals,
pubmed-meshheading:7929113-Biological Transport,
pubmed-meshheading:7929113-Cloning, Molecular,
pubmed-meshheading:7929113-Coatomer Protein,
pubmed-meshheading:7929113-Endoplasmic Reticulum,
pubmed-meshheading:7929113-Fungal Proteins,
pubmed-meshheading:7929113-Golgi Apparatus,
pubmed-meshheading:7929113-Membrane Proteins,
pubmed-meshheading:7929113-Molecular Sequence Data,
pubmed-meshheading:7929113-Mutation,
pubmed-meshheading:7929113-Saccharomyces cerevisiae,
pubmed-meshheading:7929113-Sequence Analysis, DNA,
pubmed-meshheading:7929113-Sequence Homology, Amino Acid
|
pubmed:year |
1994
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pubmed:articleTitle |
Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic.
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pubmed:affiliation |
Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|