6HLR

Yeast RNA polymerase I elongation complex bound to nucleotide analog GMPCPP (core focused)

6HLR の概要

• エントリーDOI: 10.2210/pdb6hlr/pdb
• EMDBエントリー: 0238 0239 0240
• 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, ... (18 entities in total)
• 機能のキーワード: transcription, polymerase, nucleotide, elongation
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 547362.27

構造登録者

Tafur, L.,Sadian, Y.,Weis, F.,Muller, C.W. (登録日: 2018-09-11, 公開日: 2019-04-03, 最終更新日: 2024-05-15)

主引用文献

Tafur, L.,Sadian, Y.,Hanske, J.,Wetzel, R.,Weis, F.,Muller, C.W.
The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2.
Elife, 8:-, 2019

PubMed Abstract: RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserved position at the A135 surface. Our structural and biochemical data suggest a mechanism where reversible binding of the A49-A34.5 heterodimer could contribute to the regulation of Pol I transcription initiation and elongation.

PubMed: 30913026
DOI: 10.7554/eLife.43204

実験手法

ELECTRON MICROSCOPY (3.18 Å)