ArticleNature communications2020
The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
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- Liquid-liquid phase separation and a phage-encoded inhibitor cooperatively drive transcriptional transition during phage SPO1 infection.Nucleic acids research · 2026Article
- A noncanonical RNA polymerase assembly pathway in Bacillus subtilis: α Dimer associates with either β or β' before forming the core enzyme.The Journal of biological chemistry · 2026Article
- Inherent MS-cleavability of diazirine photo-cross-links enables residue-level structural analysis.Nature communications · 2026Article
- The ω subunit stabilizes transcribing RNA polymerase to balance processivity and collision resolution.bioRxiv : the preprint server for biology · 2026Article
- Rapid photo-crosslinking in living cells reveals protein-nucleic acid dynamics on a timescale of minutes.Nucleic acids research · 2026Article
- Bacteria sense the antibiotic rifampicin through a widespread dual-promoter based alarm system.Nucleic acids research · 2026Article
- High-Level Expression of Humicola insolens Cutinase in Bacillus subtilis.Applied biochemistry and biotechnology · 2025Article
- Expanding the CarD interaction network: CrsL is a novel transcription regulator in actinobacteria.Nucleic acids research · 2025Article
- RapA opens the RNA polymerase clamp to disrupt post-termination complexes and prevent cytotoxic R-loop formation.Nature structural & molecular biology · 2025Article
- Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ.Nature communications · 2025Article
- How do bacteria tune transcription termination efficiency?Current opinion in microbiology · 2024Review
- Mycobacterial HelD connects RNA polymerase recycling with transcription initiation.Nature communications · 2024Article
- Dissecting diazirine photo-reaction mechanism for protein residue-specific cross-linking and distance mapping.Nature communications · 2024Article
- Structural basis of promoter recognition by Staphylococcus aureus RNA polymerase.Nature communications · 2024Article
- Oligomerization states of the Mycobacterium tuberculosis RNA polymerase core and holoenzymes.Archives of microbiology · 2024Article
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
- Rippling life on a dormant planet: hibernation of ribosomes, RNA polymerases, and other essential enzymes.Frontiers in microbiology · 2024Review
- What the Hel: recent advances in understanding rifampicin resistance in bacteria.FEMS microbiology reviews · 2023Article
- Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization.Nature communications · 2023Article
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Authors and funding
11 authors at 6 institutions in 4 countries.
Funding
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)
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.