ArticleNucleic acids research2007
Tfb5 interacts with Tfb2 and facilitates nucleotide excision repair in yeast.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- MoMkt1, a member of XPG/RAD2 nuclease family, regulates development and pathogenicity inVirulence · 2025Article
- The basal transcription factor II H subunit Tfb5 is required for stress response and pathogenicity in the tangerine pathotype of Alternaria alternata.Molecular plant pathology · 2020Article
- Review
- Disruption of TTDA results in complete nucleotide excision repair deficiency and embryonic lethality.PLoS genetics · 2013Article
- Physical and functional interactions between Drosophila homologue of Swc6/p18Hamlet subunit of the SWR1/SRCAP chromatin-remodeling complex with the DNA repair/transcription factor TFIIH.The Journal of biological chemistry · 2012Article
- Control of the function of the transcription and repair factor TFIIH by the action of the cochaperone Ydj1.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Slowly progressing nucleotide excision repair in trichothiodystrophy group A patient fibroblasts.Molecular and cellular biology · 2011Article
- p8/TTDA overexpression enhances UV-irradiation resistance and suppresses TFIIH mutations in a Drosophila trichothiodystrophy model.PLoS genetics · 2008Article
- Mms19 protein functions in nucleotide excision repair by sustaining an adequate cellular concentration of the TFIIH component Rad3.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Tfb5 is partially dispensable for Rad26 mediated transcription coupled nucleotide excision repair in yeast.DNA repair · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
TFIIH is indispensable for nucleotide excision repair (NER) and RNA polymerase II transcription. Its tenth subunit was recently discovered in yeast as Tfb5. Unlike other TFIIH subunits, Tfb5 is not essential for cell survival. We have analyzed the role of Tfb5 in NER. NER was deficient in the tfb5 deletion mutant cell extracts, and was specifically complemented by purified Tfb5 protein. In contrast to the extreme ultraviolet (UV) sensitivity of rad14 mutant cells that lack any NER activity, tfb5 deletion mutant cells were moderately sensitive to UV radiation, resembling that of the tfb1-101 mutant cells in which TFIIH activity is compromised but not eliminated. Thus, Tfb5 protein directly participates in NER and is an accessory NER protein that stimulates the repair to the proficient level. Lacking a DNA binding activity, Tfb5 was found to interact with the core TFIIH subunit Tfb2, but not with other NER proteins. The Tfb5-Tfb2 interaction was correlated with the cellular NER function of Tfb5, supporting the functional importance of this interaction. Our results led to a model in which Tfb5 acts as an architectural stabilizer conferring structural rigidity to the core TFIIH such that the complex is maintained in its functional architecture.
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