6H67

Yeast RNA polymerase I elongation complex stalled by cyclobutane pyrimidine dimer (CPD)

6H67 の概要

• エントリーDOI: 10.2210/pdb6h67/pdb
• EMDBエントリー: 0146
• 分子名称: DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (19 entities in total)
• 機能のキーワード: rna polymerase i, uv-damage, stalling, cyclobutane pyrimidine dimers (cpd), transcription
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 625814.71

構造登録者

Sanz-Murillo, M.,Xu, J.,Gil-Carton, D.,Wang, D.,Fernandez-Tornero, C. (登録日: 2018-07-26, 公開日: 2018-08-29, 最終更新日: 2024-05-15)

主引用文献

Sanz-Murillo, M.,Xu, J.,Belogurov, G.A.,Calvo, O.,Gil-Carton, D.,Moreno-Morcillo, M.,Wang, D.,Fernandez-Tornero, C.
Structural basis of RNA polymerase I stalling at UV light-induced DNA damage.
Proc. Natl. Acad. Sci. U.S.A., 115:8972-8977, 2018

PubMed Abstract: RNA polymerase I (Pol I) transcribes ribosomal DNA (rDNA) to produce the ribosomal RNA (rRNA) precursor, which accounts for up to 60% of the total transcriptional activity in growing cells. Pol I monitors rDNA integrity and influences cell survival, but little is known about how this enzyme processes UV-induced lesions. We report the electron cryomicroscopy structure of Pol I in an elongation complex containing a cyclobutane pyrimidine dimer (CPD) at a resolution of 3.6 Å. The structure shows that the lesion induces an early translocation intermediate exhibiting unique features. The bridge helix residue Arg1015 plays a major role in CPD-induced Pol I stalling, as confirmed by mutational analysis. These results, together with biochemical data presented here, reveal the molecular mechanism of Pol I stalling by CPD lesions, which is distinct from Pol II arrest by CPD lesions. Our findings open the avenue to unravel the molecular mechanisms underlying cell endurance to lesions on rDNA.

PubMed: 30127008
DOI: 10.1073/pnas.1802626115

実験手法

ELECTRON MICROSCOPY (3.6 Å)