ArticleNature communications2020
Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.
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 20 papers.
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Who cites it
20 citing papers in PubMed.
- Liquid-liquid phase separation and a phage-encoded inhibitor cooperatively drive transcriptional transition during phage SPO1 infection.Nucleic acids research · 2026Article
- Bacteria sense the antibiotic rifampicin through a widespread dual-promoter based alarm system.Nucleic acids research · 2026Article
- Expanding the CarD interaction network: CrsL is a novel transcription regulator in actinobacteria.Nucleic acids research · 2025Article
- Recent advances in mycobacterial transcription: insights beyond the general pathway.Journal of bacteriology · 2025Review
- MoaB2, a newly identified transcription factor, binds to σJournal of bacteriology · 2024Article
- Biochemical characterization ofJournal of bacteriology · 2024Article
- Mycobacterial HelD connects RNA polymerase recycling with transcription initiation.Nature communications · 2024Article
- RIP-seq reveals RNAs that interact with RNA polymerase and primary sigma factors in bacteria.Nucleic acids research · 2024Article
- 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
- DNA structural properties of DNA binding sites for 21 transcription factors in the mycobacterial genome.Frontiers in cellular and infection microbiology · 2023Article
- Mycobacterium abscessus HelR interacts with RNA polymerase to confer intrinsic rifamycin resistance.Molecular cell · 2022Article
- The structure and activities of the archaeal transcription termination factor Eta detail vulnerabilities of the transcription elongation complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- RNA polymerase pausing, stalling and bypass during transcription of damaged DNA: from molecular basis to functional consequences.Nucleic acids research · 2022Review
- Using cryo-EM to uncover mechanisms of bacterial transcriptional regulation.Biochemical Society transactions · 2021Review
- Multiple classes and isoforms of the RNA polymerase recycling motor protein HelD.MicrobiologyOpen · 2021Article
- β-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck.Nucleic acids research · 2021Review
- Transcription complexes as RNA chaperones.Transcription · 2021Article
- The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.Nature communications · 2020Article
- Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.Nature communications · 2020Article
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Authors and funding
20 authors.
Funding
Abstract
RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.
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