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rdf:type |
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lifeskim:mentions |
umls-concept:C0020792,
umls-concept:C0033684,
umls-concept:C1273518,
umls-concept:C1415549,
umls-concept:C1420877,
umls-concept:C1514562,
umls-concept:C1704675,
umls-concept:C1709915,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2697539
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pubmed:issue |
1
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pubmed:dateCreated |
2000-6-5
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pubmed:abstractText |
Ssn6, a yeast protein that comprises 10 tandem tetratricopeptide repeat (TPR) motifs, associates with Tup1 repressor protein and acts as a transcriptional corepressor. In this report we identify point mutations in the TPR1 of Ssn6 that disrupt Tup1 interaction. Furthermore, we construct a 3D model of the TPR domain of Ssn6, which is responsible for Tup1 binding, based on the known structure of protein phosphatase 5. According to this model all selected mutations reduce the ability of Ssn6 to interact with Tup1 by affecting the structural integrity of TPR1 and/or the correct spatial arrangement of TPR1 relative to TPR2 and TPR3.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/CYC8 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TUP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase 5
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
473
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37-41
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pubmed:dateRevised |
2009-7-23
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pubmed:meshHeading |
pubmed-meshheading:10802055-Amino Acid Motifs,
pubmed-meshheading:10802055-Amino Acid Sequence,
pubmed-meshheading:10802055-Binding Sites,
pubmed-meshheading:10802055-Crystallography, X-Ray,
pubmed-meshheading:10802055-DNA-Binding Proteins,
pubmed-meshheading:10802055-Fungal Proteins,
pubmed-meshheading:10802055-Gene Expression Regulation, Fungal,
pubmed-meshheading:10802055-Models, Molecular,
pubmed-meshheading:10802055-Molecular Sequence Data,
pubmed-meshheading:10802055-Nuclear Proteins,
pubmed-meshheading:10802055-Phosphoprotein Phosphatases,
pubmed-meshheading:10802055-Point Mutation,
pubmed-meshheading:10802055-Protein Binding,
pubmed-meshheading:10802055-Protein Structure, Secondary,
pubmed-meshheading:10802055-Protein Structure, Tertiary,
pubmed-meshheading:10802055-Repetitive Sequences, Amino Acid,
pubmed-meshheading:10802055-Repressor Proteins,
pubmed-meshheading:10802055-Saccharomyces cerevisiae,
pubmed-meshheading:10802055-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10802055-Sequence Alignment,
pubmed-meshheading:10802055-Static Electricity,
pubmed-meshheading:10802055-Structure-Activity Relationship,
pubmed-meshheading:10802055-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
Identification of residues in the TPR domain of Ssn6 responsible for interaction with the Tup1 protein.
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pubmed:affiliation |
Institute of Molecular Biology and Biotechnology-Foundation of Research and Technology, Vassilika Vouton, P.O. Box 711 10, Heraklion, Crete, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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