p53 modulation of TFIIH–associated nucleotide excision repair activity

@article{Wang1995p53MO,
  title={p53 modulation of TFIIH–associated nucleotide excision repair activity},
  author={X.-W. Wang and Hsu-Hua Yeh and Laure Schaeffer and Richard Roy and Vincent Moncollin and Jean Marc Egly and Z. Wang and Errol C. Friedberg and Michele K. Evans and Bonita G. Taffe and Vilhelm A. Bohr and Geert Weeda and Jan H. J. Hoeijmakers and Kathleen Forrester and Curtis C. Harris},
  journal={Nature Genetics},
  year={1995},
  volume={10},
  pages={188-195}
}
p53 has pleiotropic functions including control of genomic plasticity and integrity. Here we report that p53 can bind to several transcription factor IIH–associated factors, including transcription–repair factors, XPD (Rad3) and XPB, as well as CSB involved in strand–specific DNA repair, via its C–terminal domain. We also found that wild–type, but not Arg273His mutant p53 inhibits XPD (Rad3) and XPB DNA helicase activities. Moreover, repair of UV–induced dimers is slower in Li–Fraumeni syndrome… 
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    Proceedings of the National Academy of Sciences of the United States of America
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Interacts with hRAD 51 and hRAD 54 , and Directly Modulates Homologous Recombination 1 , 2
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The hypothesis that p53 helps maintain genetic stability through transcription-independent modulation of homologous recombination factors is supported.
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TLDR
It is reported that p53 physically interacts with and inhibits the function of a cellular DNA replication factor, the single-stranded DNA-binding protein complex RPA.
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TLDR
Findings suggest that transcription and nucleotide excision repair may share common factors and hence may be considered to be functionally related.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
It is found thatTFIIH has a dual role, being required for basal transcription of class II genes and for participation in DNA-excision repair, and the general transcription factor IIE negatively modulates the helicase activity of TFIIH through a direct interaction between TFIIE and the ERCC3 subunit of TF IIH.
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