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-Structure paper
タイトル | The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 6418, Year 2020 |
掲載日 | 2020年12月18日 |
著者 | Hao-Hong Pei / Tarek Hilal / Zhuo A Chen / Yong-Heng Huang / Yuan Gao / Nelly Said / Bernhard Loll / Juri Rappsilber / Georgiy A Belogurov / Irina Artsimovitch / Markus C Wahl / |
PubMed 要旨 | 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. ...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. |
リンク | Nat Commun / PubMed:33339827 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.85 - 4.23 Å |
構造データ | EMDB-11104: Bacillus subtilis RNA polymerase HelD complex 1 EMDB-11105: Bacillus subtilis RNA Polymerase complex 2 |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | TRANSCRIPTION / TRANSCRIPTION/DNA/RNA / DNA-DEPENDENT RNA POLYMERASE / BACTERIAL / Helicase |