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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
2000-10-23
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pubmed:databankReference |
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pubmed:abstractText |
TFIIS is a transcription elongation factor that consists of three domains. We have previously solved the structures of domains II and III, which stimulate arrested polymerase II elongation complexes in order to resume transcription. Domain I is conserved in evolution from yeast to human species and is homologous to the transcription factors elongin A and CRSP70. Domain I also interacts with the transcriptionally active RNA polymerase II holoenzyme and therefore, may have a function unrelated to the previously described transcription elongation activity of TFIIS. We have solved the structure of domain I of yeast TFIIS using NMR spectroscopy. Domain I is a compact four-helix bundle that is structurally independent of domains II and III of the TFIIS. Using the yeast structure as a template, we have modeled the homologous domains from elongin A and CRSP70 and identified a conserved positively charged patch on the surface of all three proteins, which may be involved in conserved functional interactions with the transcriptional machinery.
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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/CRSP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MED26 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, General,
http://linkedlifedata.com/resource/pubmed/chemical/Transcriptional Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/elongin,
http://linkedlifedata.com/resource/pubmed/chemical/transcription factor S-II
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31266-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10811649-Amino Acid Sequence,
pubmed-meshheading:10811649-Animals,
pubmed-meshheading:10811649-Cloning, Molecular,
pubmed-meshheading:10811649-Computer Simulation,
pubmed-meshheading:10811649-Conserved Sequence,
pubmed-meshheading:10811649-Fungal Proteins,
pubmed-meshheading:10811649-Humans,
pubmed-meshheading:10811649-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10811649-Mediator Complex,
pubmed-meshheading:10811649-Models, Molecular,
pubmed-meshheading:10811649-Molecular Sequence Data,
pubmed-meshheading:10811649-Protein Folding,
pubmed-meshheading:10811649-Protein Structure, Secondary,
pubmed-meshheading:10811649-Protein Structure, Tertiary,
pubmed-meshheading:10811649-Sequence Homology, Amino Acid,
pubmed-meshheading:10811649-Trans-Activators,
pubmed-meshheading:10811649-Transcription, Genetic,
pubmed-meshheading:10811649-Transcription Factors,
pubmed-meshheading:10811649-Transcription Factors, General,
pubmed-meshheading:10811649-Transcriptional Elongation Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70.
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pubmed:affiliation |
Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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