Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH

Marinoni, Jean‐Christophe; Roy, Richard; Vermeulen, Wim; Miniou, Pierre; Lutz, Yves; Weeda, Geert; Seroz, Thierry; Gomez, Denise Molina; Hoeijmakers, Jan H.J.; Egly, Jean‐Marc

doi:10.1093/emboj/16.5.1093

Cited by 68 publications

(71 citation statements)

References 35 publications

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“…This work, together with a related study on the human homolog of Tfb2 (46), completes the molecular definition of TFIIH. Due to the complexity, scarcity, and fragile nature of the complex, the effort has consumed the better part of a decade.…”

Section: Discussionsupporting

confidence: 56%

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Genes For Tfb2, Tfb3, and Tfb4 Subunits of Yeast Transcription/Repair Factor IIH

Feaver

Henry

Wang

et al. 1997

Journal of Biological Chemistry

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Genes for the Tfb2, Tfb3, and Tfb4 subunits of yeast RNA polymerase transcription factor IIH (TFIIH) are described. All three genes are essential for cell viability, and antibodies against Tfb3 specifically inhibit transcription in vitro. A C-terminal deletion of Tfb2 caused a defect in nucleotide excision repair, as shown by UV sensitivity of the mutant strain and loss of nucleotide excision repair activity in cell extracts (restored by the addition of purified TFIIH). An interaction between Tfb3 and the Kin28 subunit of TFIIH was detected by the two-hybrid approach, consistent with a role for Tfb3 in linking kinase and core domains of the factor. The deduced amino acid sequence of Tfb2 is similar to that of the 52-kDa subunit of human TFIIH, while Tfb3 is identified as a RING finger protein homologous to the 36-kDa subunit of murine CAK (cyclin-dependent kinase activating kinase) and to the 32-kDa subunit of human TFIIH. Tfb4 is homologous to p34 of human TFIIH and is identified as the weakly associated 37-kDa subunit of the yeast factor. These and other findings reveal a oneto-one correspondence and high degree of sequence similarity between the entire set of yeast and human TFIIH polypeptides.

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Section: Discussionsupporting

confidence: 56%

“…Comparison with a companion study on the human factor (46) discloses an extraordinary degree of conservation between the yeast and human proteins.…”

mentioning

confidence: 92%

Genes For Tfb2, Tfb3, and Tfb4 Subunits of Yeast Transcription/Repair Factor IIH

Feaver

Henry

Wang

et al. 1997

Journal of Biological Chemistry

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“…3 and Fig. 3C)), in 20 l of a buffer containing 50 mM Tris-HCl, pH 7.9, 10% glycerol, 0.1 mM EDTA, 0.5 mM dithiothreitol, 50 mM KCl, 5 mM MgCl 2, 60 g/ml bovine serum albumin, and 0.5 g poly(dG-dC), for 30 min at 30°C.…”

Section: Methodsmentioning

confidence: 99%

“…Although the protein composition and the nature of the different subunits are almost completely determined (Ref. 3 and references therein), relatively little is known concerning the precise functions of TFIIH in both mechanisms. However, genetic studies in yeast (4,5) and Chinese hamster ovary cells (6), as well as the association of mutations in XPB and XPD with the human disorders xeroderma pigmentosum (XP), Cockayne syndrome, and trichothiodystrophy (7,1), demonstrate the crucial importance of TFIIH in cellular DNA metabolism.…”

mentioning

confidence: 99%

DNA Damage Recognition by XPA Protein Promotes Efficient Recruitment of Transcription Factor II H

Nocentini¹,

Coin²,

Saijo³

et al. 1997

Journal of Biological Chemistry

104

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The human basal transcription factor IIH (TFIIH) is an essential component of the nucleotide excision repair machinery. TFIIH is required for reaction steps concomitant with or prior to the formation of dual incisions in the damaged DNA strand. To understand the mechanism underlying the recruitment of TFIIH to DNA damage sites we have analyzed i) the direct affinity of TFIIH for damaged or undamaged DNA and ii) the interaction of TFIIH with XPA⅐DNA complexes, formed using unirradiated or UV-irradiated DNA.Filter binding assays showed that TFIIH has some affinity for the DNA, but in contrast to XPA, does not show any preference for UV-irradiated DNA. Pull-down experiments demonstrated that TFIIH binds to XPA⅐DNA complexes in an UV damage-dependent manner by a direct protein-protein interaction with XPA. We propose that an enhancement of the affinity of XPA protein for TFIIH could arise from conformational changes of XPA when it binds to UV lesions on the DNA.Transcription initiation of protein coding genes and nucleotide excision repair (NER) 1 of damaged DNA were shown to be connected through the dual action of TFIIH, a multisubunit protein complex that contains several enzymatic activities (reviewed in Refs. 1 and 2). Although the protein composition and the nature of the different subunits are almost completely determined (Ref. 3 and references therein), relatively little is known concerning the precise functions of TFIIH in both mechanisms. However, genetic studies in yeast (4, 5) and Chinese hamster ovary cells (6), as well as the association of mutations in XPB and XPD with the human disorders xeroderma pigmentosum (XP), Cockayne syndrome, and trichothiodystrophy (7, 1), demonstrate the crucial importance of TFIIH in cellular DNA metabolism.During transcription initiation, TFIIH is thought to be recruited to a promoter, after the formation of the preinitiation complex containing TFIID, TFIIB, TFIIF, and RNA polymerase II on the TATA box consensus sequence (8). Once associated with this complex, TFIIH is likely to function through its ATPdependent helicase subunits, which may facilitate the opening of the promoter region (9) to allow the reading of the DNA. The cyclin dependent-kinase activity of TFIIH phosphorylates the carboxyl-terminal domain of RNA polymerase II in a reaction that has been proposed to activate the elongation process (10, 11). During NER, TFIIH is thought to be recruited to the damage site at an early step of the repair process (12-14). The initial recognition of DNA lesions is likely to involve a nucleoprotein⅐DNA complex consisting of XPA, a zinc finger protein with some specificity for UV-or chemical carcinogendamaged DNA (15-19), RPA (20 -24), and probably other factors. TFIIH may then be involved in the formation of a preincision complex through an interaction with the COOH terminus of XPA (25). The precise role played by TFIIH during the early reaction steps of NER is not yet certain, but the ATP-dependent helicase activities of the 6) may facilitate the formation of an open DNA com...

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“…During NER, XPB and XPD act as 3Ј-5Ј and 5Ј-3Ј ATP-dependent helicases, respectively. This bidirectional helicase activity is believed to unwind the DNA double helix around the damage before incision takes place during the process of NER (34). An intriguing finding is the physical and functional interaction of p53 with both XPB and XPD (35).…”

Section: Chronic Infection With Human Hepatitis B Virus (Hbv)mentioning

confidence: 99%

Transcriptional Regulation of the TFIIH Transcription Repair Components XPB and XPD by the Hepatitis B Virus x Protein in Liver Cells and Transgenic Liver Tissue

Jaitovich-Groisman¹,

Benlimame²,

Slagle³

et al. 2001

Journal of Biological Chemistry

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Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH

Cited by 68 publications

References 35 publications

Genes For Tfb2, Tfb3, and Tfb4 Subunits of Yeast Transcription/Repair Factor IIH

Genes For Tfb2, Tfb3, and Tfb4 Subunits of Yeast Transcription/Repair Factor IIH

DNA Damage Recognition by XPA Protein Promotes Efficient Recruitment of Transcription Factor II H

Transcriptional Regulation of the TFIIH Transcription Repair Components XPB and XPD by the Hepatitis B Virus x Protein in Liver Cells and Transgenic Liver Tissue

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