ArticleThe Journal of biological chemistry2013
Mycobacterium tuberculosis RNA polymerase-binding protein A (RbpA) and its interactions with sigma factors.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
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- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Expanding the CarD interaction network: CrsL is a novel transcription regulator in actinobacteria.Nucleic acids research · 2025Article
- Targeted protein degradation in mycobacteria uncovers antibacterial effects and potentiates antibiotic efficacy.Nature communications · 2024Article
- Compensatory mutations are associated with increasedMicrobial genomics · 2024Article
- Biophysical evolution of the receptor-binding domains of SARS-CoVs.Biophysical journal · 2023Article
- Metagenomic Insights for Antimicrobial Resistance Surveillance in Soils with Different Land Uses in Brazil.Antibiotics (Basel, Switzerland) · 2023Article
- Recent Progress and Challenges for Drug-Resistant Tuberculosis Treatment.Pharmaceutics · 2021Review
- Diverse and unified mechanisms of transcription initiation in bacteria.Nature reviews. Microbiology · 2021Review
- Transcription initiation in mycobacteria: a biophysical perspective.Transcription · 2020Review
- The σ Subunit-Remodeling Factors: An Emerging Paradigms of Transcription Regulation.Frontiers in microbiology · 2020Review
- Article
- CarD and RbpA modify the kinetics of initial transcription and slow promoter escape of the Mycobacterium tuberculosis RNA polymerase.Nucleic acids research · 2019Article
- CarD contributes to diverse gene expression outcomes throughout the genome ofProceedings 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
- 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
- Fidaxomicin jamseLife · 2018Article
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
RNA polymerase-binding protein A (RbpA), encoded by Rv2050, is specific to the actinomycetes, where it is highly conserved. In the pathogen Mycobacterium tuberculosis, RbpA is essential for growth and survival. RbpA binds to the β subunit of the RNA polymerase where it activates transcription by unknown mechanisms, and it may also influence the response of M. tuberculosis to the current frontline anti-tuberculosis drug rifampicin. Here we report the solution structure of RbpA and identify the principle sigma factor σ(A) and the stress-induced σ(B) as interaction partners. The protein has a central ordered domain with a conserved hydrophobic surface that may be a potential protein interaction site. The N and C termini are highly dynamic and are involved in the interaction with the sigma factors. RbpA forms a tight complex with the N-terminal domain of σ(B) via its N- and C-terminal regions. The interaction with sigma factors may explain how RbpA stabilizes sigma subunit binding to the core RNA polymerase and thereby promotes initiation complex formation. RbpA could therefore influence the competition between principal and alternative sigma factors and hence the transcription profile of the cell.
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Registered trials
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