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Ubiquitin ligase activity of TFIIH and the transcriptional response to DNA damage.

Authors
  • Y, Takagi
  • Ca, Masuda
  • Wh, Chang
  • H, Komori
  • D, Wang
  • Tony Hunter
  • Ca, Joazeiro
  • Rd, Kornberg
Type
Published Article
Journal
Molecular Cell
Publisher
Elsevier
Volume
18
Issue
2
Pages
237–243
Source
Hunter Lab
License
Unknown

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.

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