6ZFB

Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer)

6ZFB の概要

• エントリーDOI: 10.2210/pdb6zfb/pdb
• EMDBエントリー: 11105
• 分子名称: DNA-directed RNA polymerase subunit delta, RNA polymerase subunit omega, DNA-directed RNA polymerase subunit alpha, ... (7 entities in total)
• 機能のキーワード: transcription/dna/rna, dna-dependent rna polymerase, bacterial, transcription, helicase
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 905367.71

構造登録者

Pei, H.-P.,Hilal, T.,Huang, Y.-H.,Said, N.,Loll, B.,Wahl, M.C. (登録日: 2020-06-17, 公開日: 2020-10-14, 最終更新日: 2024-05-15)

主引用文献

Pei, H.H.,Hilal, T.,Chen, Z.A.,Huang, Y.H.,Gao, Y.,Said, N.,Loll, B.,Rappsilber, J.,Belogurov, G.A.,Artsimovitch, I.,Wahl, M.C.
The delta subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.
Nat Commun, 11:6418-6418, 2020

PubMed Abstract: Cellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains elusive. In Bacillus subtilis, the RNAP δ subunit and NTPase HelD have been implicated in RNAP recycling. We structurally analyzed Bacillus subtilis RNAP-δ-HelD complexes. HelD has two long arms: a Gre cleavage factor-like coiled-coil inserts deep into the RNAP secondary channel, dismantling the active site and displacing RNA, while a unique helical protrusion inserts into the main channel, prying the β and β' subunits apart and, aided by δ, dislodging DNA. RNAP is recycled when, after releasing trapped nucleic acids, HelD dissociates from the enzyme in an ATP-dependent manner. HelD abundance during slow growth and a dimeric (RNAP-δ-HelD) structure that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzyme pools in response to cellular cues.

PubMed: 33339827
DOI: 10.1038/s41467-020-20159-3

実験手法

ELECTRON MICROSCOPY (3.9 Å)