4WQT

Thermus thermophilus RNA polymerase complexed with an RNA cleavage stimulating factor (a GreA/Gfh1 chimeric protein)

4WQT の概要

• エントリーDOI: 10.2210/pdb4wqt/pdb
• 関連するPDBエントリー: 3AOH 3AOI 4WQS
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total)
• 機能のキーワード: transcription, rna cleavage, transferase-transcription complex, transferase/transcription
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 1186514.37

構造登録者

Murayama, Y.,Sekine, S.,Yokoyama, S. (登録日: 2014-10-22, 公開日: 2015-02-18, 最終更新日: 2024-03-20)

主引用文献

Sekine, S.I.,Murayama, Y.,Svetlov, V.,Nudler, E.,Yokoyama, S.
The Ratcheted and Ratchetable Structural States of RNA Polymerase Underlie Multiple Transcriptional Functions.
Mol.Cell, 57:408-421, 2015

PubMed Abstract: DNA-dependent RNA polymerase (RNAP) accomplishes multiple tasks during transcription by assuming different structural forms. Reportedly, the "tight" form performs nucleotide addition to nascent RNA, while the "ratcheted" form is adopted for transcription inhibition. In this study, we performed Cys-pair crosslinking (CPX) analyses of various transcription complexes of a bacterial RNAP and crystallographic analyses of its backtracked and Gre-factor-bound states to clarify which of the two forms is adopted. The ratcheted form was revealed to support GreA-dependent transcript cleavage, long backtracking, hairpin-dependent pausing, and termination. In contrast, the tight form correlated with nucleotide addition, mismatch-dependent pausing, one-nucleotide backtracking, and factor-independent transcript cleavage. RNAP in the paused/backtracked state, but not the nucleotide-addition state, readily transitions to the ratcheted form ("ratchetable"), indicating that the tight form represents two distinct regulatory states. The 3' end and the hairpin structure of the nascent RNA promote the ratchetable nature by modulating the trigger-loop conformation.

PubMed: 25601758
DOI: 10.1016/j.molcel.2014.12.014

実験手法

X-RAY DIFFRACTION (4.4 Å)