2LOX

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

2LOX の概要

• エントリーDOI: 10.2210/pdb2lox/pdb
• 関連するPDBエントリー: 1Y5O 2GS0 2K2U 2L2I
• NMR情報: BMRB: 18229
• 分子名称: RNA polymerase II transcription factor B subunit 1, DNA repair protein RAD2 (2 entities in total)
• 機能のキーワード: transcription-hydrolase complex, transcription/hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus: P32776 P07276
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19263.26

構造登録者

Lafrance-Vanasse, J.,Legault, P.,Omichinski, J. (登録日: 2012-01-27, 公開日: 2012-02-15, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR