ArticleStructure (London, England : 1993)2014
Structure of the DNA-binding and RNA-polymerase-binding region of transcription antitermination factor λQ.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- In transcription antitermination by Qλ, NusA induces refolding of Qλ to form a nozzle that extends the RNA polymerase RNA-exit channel.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of AlpA-dependent transcription antitermination.Nucleic acids research · 2022Article
- NusA directly interacts with antitermination factor Q from phage λ.Scientific reports · 2020Article
- Structural basis of Q-dependent antitermination.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural basis of Q-dependent transcription antitermination.Nature communications · 2019Article
- Article
- N protein from lambdoid phages transforms NusA into an antiterminator by modulating NusA-RNA polymerase flap domain interactions.Nucleic acids research · 2015Article
- Bacteriophage lambda: Early pioneer and still relevant.Virology · 2015Review
- Molecular basis of RNA polymerase promoter specificity switch revealed through studies ofBacteriophage · 2014Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
The bacteriophage λ Q protein is a transcription antitermination factor that controls expression of the phage late genes as a stable component of the transcription elongation complex. To join the elongation complex, λQ binds a specific DNA sequence element and interacts with RNA polymerase that is paused during early elongation. λQ binds to the paused early-elongation complex through interactions between λQ and two regions of RNA polymerase: region 4 of the σ(70) subunit and the flap region of the β subunit. We present the 2.1 Å resolution crystal structure of a portion of λQ containing determinants for interaction with DNA, interaction with region 4 of σ(70), and interaction with the β flap. The structure provides a framework for interpreting prior genetic and biochemical analysis and sets the stage for future structural studies to elucidate the mechanism by which λQ alters the functional properties of the transcription elongation complex.
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