2lox

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NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2

Structural highlights

2lox is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2gs0, 2l2i, 1y5o, 2k2u
Gene:	D9740.3, TFB1, YDR311W (Saccharomyces cerevisiae), RAD2, YGR258C (Saccharomyces cerevisiae)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TFB1_YEAST] Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro.^[1] ^[2] [RAD2_YEAST] Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair.^[3]

Publication Abstract from PubMed

The general transcription factor IIH (TFIIH) plays crucial roles in transcription as part of the pre-initiation complex (PIC) and in DNA repair as part of the nucleotide excision repair (NER) machinery. During NER, TFIIH recruits the 3'-endonuclease Rad2 to damaged DNA. In this manuscript, we functionally and structurally characterized the interaction between the Tfb1 subunit of TFIIH and Rad2. We show that deletion of either the PH domain of Tfb1 (Tfb1PH) or several segments of the Rad2 spacer region yield yeast with enhanced sensitivity to UV irradiation. Isothermal titration calorimetry studies demonstrate that two acidic segments of the Rad2 spacer bind to Tfb1PH with nanomolar affinity. Structure determination of a Rad2-Tfb1PH complex indicates that Rad2 binds to TFIIH using a similar motif as TFIIEalpha uses to bind TFIIH in the PIC. Together, these results provide a mechanistic bridge between the role of TFIIH in transcription and DNA repair.

Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2.,Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG Nucleic Acids Res. 2012 Feb 28. PMID:22373916^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Svejstrup JQ, Feaver WJ, LaPointe J, Kornberg RD. RNA polymerase transcription factor IIH holoenzyme from yeast. J Biol Chem. 1994 Nov 11;269(45):28044-8. PMID:7961739
↑ Sung P, Guzder SN, Prakash L, Prakash S. Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair. J Biol Chem. 1996 May 3;271(18):10821-6. PMID:8631896
↑ Habraken Y, Sung P, Prakash L, Prakash S. Yeast excision repair gene RAD2 encodes a single-stranded DNA endonuclease. Nature. 1993 Nov 25;366(6453):365-8. PMID:8247134 doi:http://dx.doi.org/10.1038/366365a0
↑ Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. Nucleic Acids Res. 2012 Feb 28. PMID:22373916 doi:10.1093/nar/gks194