Strong Functional Interactions of TFIIH with XPC and XPG in Human DNA Nucleotide Excision Repair, without a Preassembled Repairosome

doi:10.1128/MCB.21.7.2281-2291.2001

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Molecular and Cellular Biology, April 2001, p. 2281-2291, Vol. 21, No. 7
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.7.2281-2291.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Strong Functional Interactions of TFIIH with XPC and XPG in Human DNA Nucleotide Excision Repair, without a Preassembled Repairosome

Sofia J. Araújo,¹^,² Erich A. Nigg,³ and Richard D. Wood¹^,^*

Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD,¹ and MRC Centre for Developmental Neurobiology, New Hunt's House, King's College London, Guy's Hospital Campus, London SE1 1UL,² United Kingdom, and Department of Cell Biology, Max-Planck Institute for Biochemistry, D-82152 Martinsried, Germany³

Received 6 December 2000/Returned for modification 9 January 2001/Accepted 16 January 2001

In mammalian cells, the core factors involved in the damage recognition and incision steps of DNA nucleotide excision repairare XPA, TFIIH complex, XPC-HR23B, replication protein A (RPA),XPG, and ERCC1-XPF. Many interactions between these componentshave been detected, using different physical methods, in humancells and for the homologous factors in Saccharomyces cerevisiae.Several human nucleotide excision repair (NER) complexes, includinga high-molecular-mass repairosome complex, have been proposed.However, there have been no measurements of activity of any mammalianNER protein complex isolated under native conditions. In orderto assess relative strengths of interactions between NER factors,we captured TFIIH from cell extracts with an anti-cdk7 antibody,retaining TFIIH in active form attached to magnetic beads. Coimmunoprecipitationof other NER proteins was then monitored functionally in a reconstitutedrepair system with purified proteins. We found that all detectableTFIIH in gently prepared human cell extracts was present in theintact nine-subunit form. There was no evidence for a repair complexthat contained all of the NER components. At low ionic strengthTFIIH could associate with functional amounts of each NER factorexcept RPA. At physiological ionic strength, TFIIH associatedwith significant amounts of XPC-HR23B and XPG but not other repairfactors. The strongest interaction was between TFIIH and XPC-HR23B,indicating a coupled role of these proteins in early steps ofrepair. A panel of antibodies was used to estimate that thereare on the order of 10⁵ molecules of each core NER factor per HeLacell.

^* Corresponding author. Present address: University of Pittsburgh Cancer Institute, S867 Scaife Hall, 3550 Terrace St., Pittsburgh,PA 15261. Phone: (412) 648-9248.

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