2LOX

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

Summary for 2LOX

• Entry DOI: 10.2210/pdb2lox/pdb
• Related: 1Y5O 2GS0 2K2U 2L2I
• NMR Information: BMRB: 18229
• Descriptor: RNA polymerase II transcription factor B subunit 1, DNA repair protein RAD2 (2 entities in total)
• Functional Keywords: transcription-hydrolase complex, transcription/hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P32776 P07276
• Total number of polymer chains: 2
• Total formula weight: 19263.26

Authors

Lafrance-Vanasse, J.,Legault, P.,Omichinski, J. (deposition date: 2012-01-27, release date: 2012-02-15, Last modification date: 2024-05-15)

Primary citation

Lafrance-Vanasse, J.,Arseneault, G.,Cappadocia, L.,Chen, H.T.,Legault, P.,Omichinski, J.G.
Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2.
Nucleic Acids Res., 40:5739-5750, 2012

PubMed Abstract: 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 TFIIEα uses to bind TFIIH in the PIC. Together, these results provide a mechanistic bridge between the role of TFIIH in transcription and DNA repair.

PubMed: 22373916
DOI: 10.1093/nar/gks194

Experimental method

SOLUTION NMR