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rdf:type |
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lifeskim:mentions |
umls-concept:C0012860,
umls-concept:C0040649,
umls-concept:C0172237,
umls-concept:C0871261,
umls-concept:C1150685,
umls-concept:C1333357,
umls-concept:C1415344,
umls-concept:C1415345,
umls-concept:C1704632,
umls-concept:C1705468,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
2
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pubmed:dateCreated |
2005-4-19
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pubmed:abstractText |
Core transcription factor (TF) IIH purified from yeast possesses an E3 ubiquitin (Ub) ligase activity, which resides, at least in part, in a RING finger (RNF) domain of the Ssl1 subunit. Yeast strains mutated in the Ssl1 RNF domain are sensitive to ultraviolet (UV) light and to methyl methanesulfonate (MMS). This increased sensitivity to DNA-damaging agents does not reflect a deficiency in nucleotide excision repair. Rather, it correlates with reduced transcriptional induction of genes involved in DNA repair, suggesting that the E3 Ub ligase activity of TFIIH mediates the transcriptional response to DNA damage.
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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 |
Apr
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
237-43
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15837426-Amino Acid Sequence,
pubmed-meshheading:15837426-Cell Extracts,
pubmed-meshheading:15837426-DNA Damage,
pubmed-meshheading:15837426-Dose-Response Relationship, Drug,
pubmed-meshheading:15837426-Dose-Response Relationship, Radiation,
pubmed-meshheading:15837426-Gene Deletion,
pubmed-meshheading:15837426-Glutathione Transferase,
pubmed-meshheading:15837426-Methyl Methanesulfonate,
pubmed-meshheading:15837426-Molecular Sequence Data,
pubmed-meshheading:15837426-Mutagenesis, Site-Directed,
pubmed-meshheading:15837426-Mutagens,
pubmed-meshheading:15837426-Mutation,
pubmed-meshheading:15837426-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:15837426-Protein Structure, Tertiary,
pubmed-meshheading:15837426-Recombinant Fusion Proteins,
pubmed-meshheading:15837426-Saccharomyces cerevisiae,
pubmed-meshheading:15837426-Sequence Homology, Amino Acid,
pubmed-meshheading:15837426-Transcription, Genetic,
pubmed-meshheading:15837426-Transcription Factor TFIIH,
pubmed-meshheading:15837426-Transcription Factors, TFII,
pubmed-meshheading:15837426-Ubiquitin-Protein Ligases,
pubmed-meshheading:15837426-Ultraviolet Rays
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pubmed:year |
2005
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pubmed:articleTitle |
Ubiquitin ligase activity of TFIIH and the transcriptional response to DNA damage.
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pubmed:affiliation |
Department of Structural Biology, School of Medicine, Stanford University, Stanford, California 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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