The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK
Open accessAbstract
During human nucleotide excision repair, damage is recognized, two incisions are made flanking a DNA lesion, and residues are replaced by repair synthesis. A set of proteins required for repair of most lesions is RPA, XPA, TFIIH, XPC–hHR23B, XPG, and ERCC1–XPF, but additional components have not been excluded. The most complex and difficult to analyze factor is TFIIH, which has a 6-subunit core (XPB, XPD, p44, p34, p52, p62) and a 3-subunit kinase (CAK). TFIIH has roles both in basal transcription initiation and in DNA repair, and several inherited human disorders are associated with mutations in TFIIH subunits. To identify the forms of TFIIH that can function in repair, recombinant XPA, RPA, XPC–hHR23B, XPG, and ERCC1–XPF were combined with TFIIH fractions purified from HeLa cells. Repair activity coeluted with the peak of TFIIH and with transcription activity. TFIIH from cells with XPB or XPD mutations was defective in supporting repair, whereas TFIIH from spinal muscular atrophy cells with a deletion of one p44 gene was active. Recombinant TFIIH also functioned in repair, both a 6- and a 9-subunit form containing CAK. The CAK kinase inhibitor H-8 improved repair efficiency, indicating that CAK can negatively regulate NER by phosphorylation. The 15 recombinant polypeptides define the minimal set of proteins required for dual incision of DNA containing a cisplatin adduct. Complete repair was achieved by including highly purified human DNA polymerase δ or ε, PCNA, RFC, and DNA ligase I in reaction mixtures, reconstituting adduct repair for the first time with recombinant incision factors and human replication proteins.
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Cites
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Self-citationThe MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor
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Research works printed but not linked: 1
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Cited by
Nucleotide Excision Repair in Eukaryotes
Scharer, O. D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012609 · Cited by 801
DNA repair mechanisms in dividing and non-dividing cells
Iyama, T., & Wilson, D. M. (2013) · DNA Repair · doi:10.1016/j.dnarep.2013.04.015 · Cited by 697
Molecular Mechanisms of Mammalian Global Genome Nucleotide Excision Repair
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UV-Induced Ubiquitylation of XPC Protein Mediated by UV-DDB-Ubiquitin Ligase Complex
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Fousteri, M., & Mullenders, L. H. (2008) · Cell Research · doi:10.1038/cr.2008.6 · Cited by 487
Metadata
- Authors
- Araújo, S. J., Tirode, F., Coin, F., Pospiech, H., Syväoja, J. E., Stucki, M., Hübscher, U., Egly, J.-M., & Wood, R. D.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-02-01
- Volume
- 14
- Issue
- 3
- Pages
- 349-359
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W1886853229
- Cited by
- 335
- References
- 62
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Araújo, S. J., Tirode, F., Coin, F., Pospiech, H., Syväoja, J. E., Stucki, M., Hübscher, U., Egly, J.-M., & Wood, R. D. (2000). Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK. Genes & Development. https://doi.org/10.1101/gad.14.3.349
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