ArticleNucleic acids research2014
Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- Bacteria sense the antibiotic rifampicin through a widespread dual-promoter based alarm system.Nucleic acids research · 2026Article
- Mycobacterial HelD connects RNA polymerase recycling with transcription initiation.Nature communications · 2024Article
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
- What the Hel: recent advances in understanding rifampicin resistance in bacteria.FEMS microbiology reviews · 2023Article
- Mycobacterium abscessus HelR interacts with RNA polymerase to confer intrinsic rifamycin resistance.Molecular cell · 2022Article
- Article
- 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
- RNA polymerases from low G+C gram-positive bacteria.Transcription · 2021Review
- Quasi-essentiality of RNase Y in Bacillus subtilis is caused by its critical role in the control of mRNA homeostasis.Nucleic acids research · 2021Article
- A Bacteriophage DNA Mimic Protein Employs a Non-specific Strategy to Inhibit the Bacterial RNA Polymerase.Frontiers in microbiology · 2021Article
- Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.Nature communications · 2020Article
- Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.Nature communications · 2020Article
- The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.Nature communications · 2020Article
- The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes.The EMBO journal · 2020Article
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- Article
- Solution structure of domain 1.1 of the σThe Journal of biological chemistry · 2017Article
- In-Culture Cross-Linking of Bacterial Cells Reveals Large-Scale Dynamic Protein-Protein Interactions at the Peptide Level.Journal of proteome research · 2017Article
- The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial RNA polymerase (RNAP) is an essential multisubunit protein complex required for gene expression. Here, we characterize YvgS (HelD) from Bacillus subtilis, a novel binding partner of RNAP. We show that HelD interacts with RNAP-core between the secondary channel of RNAP and the alpha subunits. Importantly, we demonstrate that HelD stimulates transcription in an ATP-dependent manner by enhancing transcriptional cycling and elongation. We demonstrate that the stimulatory effect of HelD can be amplified by a small subunit of RNAP, delta. In vivo, HelD is not essential but it is required for timely adaptations of the cell to changing environment. In summary, this study establishes HelD as a valid component of the bacterial transcription machinery.
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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.