| Literature DB >> 15837426 |
Yuichiro Takagi1, Claudio A Masuda, Wei-Hau Chang, Hirofumi Komori, Dong Wang, Tony Hunter, Claudio A P Joazeiro, Roger D Kornberg.
Abstract
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.Entities:
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Year: 2005 PMID： 15837426 DOI： 10.1016/j.molcel.2005.03.007
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970