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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2005-8-8
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pubmed:databankReference |
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pubmed:abstractText |
In Saccharomyces cerevisiae, the SIF2 gene product is an integral component of the Set3 complex (SET3C), an assembly of proteins with some homology to the human SMRT and N-CoR corepressor complexes. SET3C has histone deacetylase activity that is responsible for repressing a set of meiotic genes. We have determined the X-ray crystal structure of a 46 kDa C-terminal domain of a SET3C core protein, Sif2p to 1.55 A resolution and a crystallographic R-factor of 19.0%. This domain contains an unusual eight-bladed beta-propeller structure, which differs from other transcriptional corepressor structures such as yeast Tup1p and human groucho (Gro)/TLE1, which have only seven. We have demonstrated intact Sif2p is a tetramer and the N-terminal LisH (Lis-homology)-containing domain mediates tetramerization and interaction with another component of SET3C, Snt1p. Multiple sequence alignments indicate that a surface on the "top" of the protein is conserved among species, suggesting that it may play a common role in binding partner proteins. Since Sif2p appears to be the yeast homolog of human TBL1 and TBLR1, which function in the N-CoR/SMRT complexes, its structural and oligomeric properties are likely to be very similar.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
351
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
923-35
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16051270-Amino Acid Sequence,
pubmed-meshheading:16051270-Base Sequence,
pubmed-meshheading:16051270-Binding Sites,
pubmed-meshheading:16051270-Conserved Sequence,
pubmed-meshheading:16051270-Crystallography, X-Ray,
pubmed-meshheading:16051270-DNA, Fungal,
pubmed-meshheading:16051270-Histone Deacetylases,
pubmed-meshheading:16051270-Humans,
pubmed-meshheading:16051270-Models, Molecular,
pubmed-meshheading:16051270-Molecular Sequence Data,
pubmed-meshheading:16051270-Multiprotein Complexes,
pubmed-meshheading:16051270-Protein Binding,
pubmed-meshheading:16051270-Protein Structure, Tertiary,
pubmed-meshheading:16051270-Recombinant Proteins,
pubmed-meshheading:16051270-Repetitive Sequences, Amino Acid,
pubmed-meshheading:16051270-Repressor Proteins,
pubmed-meshheading:16051270-Saccharomyces cerevisiae,
pubmed-meshheading:16051270-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16051270-Sequence Homology, Amino Acid
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pubmed:year |
2005
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pubmed:articleTitle |
The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex.
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pubmed:affiliation |
Section of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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