EMD-11104

Single-particle
4.23 Å
EMD-11104 Deposition: 29/05/2020
Map released: 14/10/2020
Last modified: 28/04/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-11104

Bacillus subtilis RNA polymerase HelD complex 1

EMD-11104

Single-particle
4.23 Å
EMD-11104 Deposition: 29/05/2020
Map released: 14/10/2020
Last modified: 28/04/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Bacillus subtilis
Sample: Recycling complex of Bacillus subitilis RNAP with HelD

Deposition Authors: Pei H, Hilal T, Huang Y, Said N, Loll B, Wahl MC
The delta subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.
Pei HH , Hilal T , Chen ZA, Huang YH , Gao Y, Said N , Loll B , Rappsilber J , Belogurov GA , Artsimovitch I , Wahl MC
(2020) Nat Commun , 11 , 6418 - 6418
PUBMED: 33339827
DOI: doi:10.1038/s41467-020-20159-3
ISSN: 2041-1723
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)2 structure that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzyme pools in response to cellular cues.