ArticleProceedings of the National Academy of Sciences of the United States of America2009
The bacteriophage T4 AsiA protein contacts the beta-flap domain of RNA polymerase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- Transcriptional reprogramming by bacteriophage T4: turning the host transcriptional machinery to the dark side.EcoSal Plus · 2025Review
- Diversity of σJournal of bacteriology · 2023Article
- Context-Dependent Action of Scc4 Reinforces Control of the Type III Secretion System.Journal of bacteriology · 2020Article
- Structural basis of σ appropriation.Nucleic acids research · 2019Article
- A novel RNA polymerase-binding protein that interacts with a sigma-factor docking site.Molecular microbiology · 2017Article
- Exploring the Amino Acid Residue Requirements of the RNA Polymerase (RNAP) α Subunit C-Terminal Domain for Productive Interaction between Spx and RNAP of Bacillus subtilis.Journal of bacteriology · 2017Article
- Environmental T4-Family Bacteriophages Evolve to Escape Abortive Infection via Multiple Routes in a Bacterial Host Employing "Altruistic Suicide" through Type III Toxin-Antitoxin Systems.Frontiers in microbiology · 2017Article
- Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase.Nucleic acids research · 2016Article
- A bacteriophage transcription regulator inhibits bacterial transcription initiation by σ-factor displacement.Nucleic acids research · 2014Article
- Structural basis for promoter specificity switching of RNA polymerase by a phage factor.Genes & development · 2014Article
- Architecture of the bacteriophage T4 activator MotA/promoter DNA interaction during sigma appropriation.The Journal of biological chemistry · 2013Article
- Insights from the architecture of the bacterial transcription apparatus.Journal of structural biology · 2012Article
- Bacteriophage T4 MotA activator and the β-flap tip of RNA polymerase target the same set of σ70 carboxyl-terminal residues.The Journal of biological chemistry · 2011Article
- A mutation within the β subunit of Escherichia coli RNA polymerase impairs transcription from bacteriophage T4 middle promoters.Journal of bacteriology · 2010Article
- Transcriptional control in the prereplicative phase of T4 development.Virology journal · 2010Review
- Molecular interactions and protein-induced DNA hairpin in the transcriptional control of bacteriophage ø29 DNA.International journal of molecular sciences · 2010Review
- Direct activator/co-activator interaction is essential for bacteriophage T4 middle gene expression.Molecular microbiology · 2009Article
- A regulator from Chlamydia trachomatis modulates the activity of RNA polymerase through direct interaction with the beta subunit and the primary sigma subunit.Genes & development · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
To initiate transcription from specific promoters, the bacterial RNA polymerase (RNAP) core enzyme must associate with the initiation factor sigma, which contains determinants that allow sequence-specific interactions with promoter DNA. Most bacteria contain several sigma factors, each of which directs recognition of a distinct set of promoters. A large and diverse family of proteins known as "anti-sigma factors" regulates promoter utilization by targeting specific sigma factors. The founding member of this family is the AsiA protein of bacteriophage T4. AsiA specifically targets the primary sigma factor in Escherichia coli, sigma(70), and inhibits transcription from the major class of sigma(70)-dependent promoters. AsiA-dependent transcription inhibition has been attributed to a well-documented interaction between AsiA and conserved region 4 of sigma(70). Here, we establish that efficient AsiA-dependent transcription inhibition also requires direct protein-protein contact between AsiA and the RNAP core. In particular, we demonstrate that AsiA contacts the flap domain of the RNAP beta-subunit (the beta-flap). Our findings support the emerging view that the beta-flap is a target site for regulatory proteins that affect RNAP function during all stages of the transcription cycle.
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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.