p53 modulation of TFIIH–associated nucleotide excision repair activity

X. W. Wang; H. Yeh; L. Schaeffer; R. Roy; V. Moncollin; J. M. Egly; Z. Wang; E. C. Friedberg; M. K. Evans; B. G. Taffe; V. A. Bohr; G. Weeda; J. H.J. Hoeijmakers; K. Forrester; C. C. Harris

doi:10.1038/ng0695-188

p53 modulation of TFIIH–associated nucleotide excision repair activity

X. W. Wang, H. Yeh, L. Schaeffer, R. Roy, V. Moncollin, J. M. Egly, Z. Wang, E. C. Friedberg, M. K. Evans, B. G. Taffe, V. A. Bohr, G. Weeda, J. H.J. Hoeijmakers, K. Forrester, C. C. Harris

Onderzoeksoutput: Bijdrage aan tijdschrift › Artikel › peer review

518 Citaten (Scopus)

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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 cells (heterozygote p53 mutant) than in normal human cells. Our findings indicate that p53 may play a direct role in modulating nucleotide excision repair pathways.

Originele taal-2	Engels
Pagina's (van-tot)	188-195
Aantal pagina's	8
Tijdschrift	Nature Genetics
Volume	10
Nummer van het tijdschrift	2
DOI's	https://doi.org/10.1038/ng0695-188
Status	Gepubliceerd - jun. 1995
Extern gepubliceerd	Ja

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title = "p53 modulation of TFIIH–associated nucleotide excision repair activity",

abstract = "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 cells (heterozygote p53 mutant) than in normal human cells. Our findings indicate that p53 may play a direct role in modulating nucleotide excision repair pathways.",

author = "Wang, {X. W.} and H. Yeh and L. Schaeffer and R. Roy and V. Moncollin and Egly, {J. M.} and Z. Wang and Friedberg, {E. C.} and Evans, {M. K.} and Taffe, {B. G.} and Bohr, {V. A.} and G. Weeda and Hoeijmakers, {J. H.J.} and K. Forrester and Harris, {C. C.}",

year = "1995",

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doi = "10.1038/ng0695-188",

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T1 - p53 modulation of TFIIH–associated nucleotide excision repair activity

AU - Wang, X. W.

AU - Yeh, H.

AU - Schaeffer, L.

AU - Roy, R.

AU - Moncollin, V.

AU - Egly, J. M.

AU - Wang, Z.

AU - Friedberg, E. C.

AU - Evans, M. K.

AU - Taffe, B. G.

AU - Bohr, V. A.

AU - Weeda, G.

AU - Hoeijmakers, J. H.J.

AU - Forrester, K.

AU - Harris, C. C.

PY - 1995/6

Y1 - 1995/6

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AB - 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 cells (heterozygote p53 mutant) than in normal human cells. Our findings indicate that p53 may play a direct role in modulating nucleotide excision repair pathways.

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JO - Nature Genetics

JF - Nature Genetics

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p53 modulation of TFIIH–associated nucleotide excision repair activity

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