2lox | pdb_00002lox
NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2
Structural highlights
FunctionTFB1_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] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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