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extensive molecular analyses unveiled that wild-type TFIIH (show GTF2H4 Proteins) cooperated in an ATP-dependent manner with PGC1-alpha as well as with the deacetylase SIRT1 (show SIRT1 Proteins), thereby contributing to the PGC1-a deacetylation by SIRT1 (show SIRT1 Proteins)
Mutations in TFIIH (show GTF2H4 Proteins) causing trichothiodystrophy are responsible for defects in ribosomal RNA production and processing.
Data show that that B2 RNA, when present with Pol II in promoter-bound complexes, specifically represses CTD phosphorylation by TFIIH (show GTF2H4 Proteins).
Molecular analyses performed on the mice brain tissue demonstrate that TFIIH (show GTF2H4 Proteins) is required for the stabilization of thyroid hormone (show PTH Proteins) receptors (TR) to their DNA-responsive elements.
Low levels of GTF2H5 are associated with enhanced prognosis in high-grade serous ovarian cancer patients and may contribute to cisplatin sensitization.
Transcriptional differences found between various TFIIH subunit (show GTF2H4 Proteins) variants participate in the phenotypic variability observed among xeroderma pigmentosum, XP associated with Cockayne syndrome, and trichothiodystrophy individuals.
Findings give new insights into the behavior of TTDA within the context of a living cell and thereby shed light on the complex phenotype of TTD-A patients.
p8/TTD-A, the tenth subunit of TFIIH (show GTF2H1 Proteins), has a critical role in DNA repair where it triggers DNA opening by stimulating XPB ATPase activity together with the damage recognition factor XPC (show XPC Proteins)-hHR23B (show RAD23B Proteins).
TTDA is the first Transcription Factor IIH subunit with a primarily nucleotide excision repair-dedicated role in vivo.
The solution structure of the p8/TTD-A protein, a small alpha/beta protein built around an antiparallel beta-sheet that forms a homodimer with an extended interface, is reported.
The data demonstrate that dMYC repression and dMYC-dependent overgrowth in the Hfp hypomorph is further impaired in the C-terminal Hay/XPB mutant background.
analysis of 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
regulation of dmyc requires interaction between the transcriptional repressor Hfp and the DNA helicase subunit of TFIIH, Haywire (Hay)
Drosophila TFIIH (hay) has roles in DNA repair and transcription
TFIIH is a basal transcription factor, but mutations in the subunit encoded by hay have specific effects in the transcription of some genes.
TFIIH core is initially located in the cytoplasm of syncytial blastoderm embryos, and that after mitotic division ten and until the cellular blastoderm stage, the core moves from the cytoplasm to the nucleus.
This gene encodes a subunit of transcription/repair factor TFIIH, which functions in gene transcription and DNA repair. This protein stimulates ERCC3/XPB ATPase activity to trigger DNA opening during DNA repair, and is implicated in regulating cellular levels of TFIIH. Mutations in this gene result in trichothiodystrophy, complementation group A.
general transcription factor IIH, polypeptide 5
, general transcription factor IIH subunit 5
, TFIIH basal transcription factor complex p34 subunit
, basic transcription factor 2 34 kDa subunit
, general transcription factor IIH subunit 3
, general transcription factor IIH, polypeptide 3, 34kDa
, general transcription factor IIH subunit 4
, TFB5 ortholog
, TFIIH basal transcription factor complex TTD-A subunit
, TFIIH basal transcription factor complex TTDA subunit
, general transcription factor IIH polypeptide 5