The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling

Hao-Hong Pei, Tarek Hilal, Zhuo A. Chen, Yong-Heng Huang, Yuan Gao, Nelly Said, Bernhard Loll, Juri Rappsilber, Georgiy A. Belogurov, Irina Artsimovitch and Markus C. Wahl ()
Additional contact information
Hao-Hong Pei: Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin
Tarek Hilal: Institute of Chemistry and Biochemistry, Research Center of Electron Microscopy and Core Facility BioSupraMol, Freie Universität Berlin
Zhuo A. Chen: Bioanalytics, Institute of Biotechnology, Technische Universität Berlin
Yong-Heng Huang: Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin
Yuan Gao: Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin
Nelly Said: Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin
Bernhard Loll: Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin
Juri Rappsilber: Bioanalytics, Institute of Biotechnology, Technische Universität Berlin
Georgiy A. Belogurov: Department of Biochemistry, University of Turku
Irina Artsimovitch: Department of Microbiology and Center for RNA Biology, The Ohio State University
Markus C. Wahl: Laboratory of Structural Biochemistry, Institute of Chemistry and Biochemistry, Freie Universität Berlin

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: 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.

Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-020-20159-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-20159-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-020-20159-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().