ArticleNucleic acids research2013
The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 48 citations in OpenAlex.
- Actinobacteria TFDB: An integrated view of transcription factors in Actinobacteria.Engineering microbiology · 2026Article
- Modular toolkit to facilitate molecular manipulations in mycobacteria.Journal of bacteriology · 2026Article
- DNA Binding by BosR Controls RpoS-Dependent and -Independent Gene Expression in Borrelia burgdorferi.Molecular microbiology · 2026Article
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Stage-associated enrichment ofFrontiers in veterinary science · 2026Article
- Single-stranded DNA drives σ subunit loading onto mycobacterial RNA polymerase to unlock initiation-competent conformations.Nucleic acids research · 2025Article
- Comparative Proteomic Analysis of Transcriptional and Regulatory Proteins Abundances inInternational journal of molecular sciences · 2022Article
- Structural basis of Streptomyces transcription activation by zinc uptake regulator.Nucleic acids research · 2022Article
- RIViT-seq enables systematic identification of regulons of transcriptional machineries.Nature communications · 2022Article
- The DUF1013 protein TrcR tracks with RNA polymerase to control the bacterial cell cycle and protect against antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Diverse and unified mechanisms of transcription initiation in bacteria.Nature reviews. Microbiology · 2021Review
- Transcription initiation in mycobacteria: a biophysical perspective.Transcription · 2020Review
- Lysine acetylation of the housekeeping sigma factor enhances the activity of the RNA polymerase holoenzyme.Nucleic acids research · 2020Article
- The σ Subunit-Remodeling Factors: An Emerging Paradigms of Transcription Regulation.Frontiers in microbiology · 2020Review
- Structural basis for transcription activation by Crl through tethering of σProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mycobacterial SigA and SigB Cotranscribe Essential Housekeeping Genes during Exponential Growth.mBio · 2019Article
- DNA mapping and kinetic modeling of the HrdB regulon in Streptomyces coelicolor.Nucleic acids research · 2019Article
- RbpA relaxes promoter selectivity of M. tuberculosis RNA polymerase.Nucleic acids research · 2018Article
- Domains within RbpA Serve Specific Functional Roles That Regulate the Expression of Distinct Mycobacterial Gene Subsets.Journal of bacteriology · 2018Article
- Single-molecule analysis reveals the mechanism of transcription activation inScience advances · 2018Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
RbpA is a small non-DNA-binding transcription factor that associates with RNA polymerase holoenzyme and stimulates transcription in actinobacteria, including Streptomyces coelicolor and Mycobacterium tuberculosis. RbpA seems to show specificity for the vegetative form of RNA polymerase as opposed to alternative forms of the enzyme. Here, we explain the basis of this specificity by showing that RbpA binds directly to the principal σ subunit in these organisms, but not to more diverged alternative σ factors. Nuclear magnetic resonance spectroscopy revealed that, although differing in their requirement for structural zinc, the RbpA orthologues from S. coelicolor and M. tuberculosis share a common structural core domain, with extensive, apparently disordered, N- and C-terminal regions. The RbpA-σ interaction is mediated by the C-terminal region of RbpA and σ domain 2, and S. coelicolor RbpA mutants that are defective in binding σ are unable to stimulate transcription in vitro and are inactive in vivo. Given that RbpA is essential in M. tuberculosis and critical for growth in S. coelicolor, these data support a model in which RbpA plays a key role in the σ cycle in actinobacteria.
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Registered trials
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.