Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda - Wikidata - awgldk - TriplyDB

Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda

Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda

http://www.wikidata.org/entity/Q34408409

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Transcription attenuation: once viewed as a novel regulatory strategy A new look at bacteriophage lambda genetic networks The structure of the coliphage HK022 Nun protein-lambda-phage boxB RNA complex. Implications for the mechanism of transcription termination Structural mimicry in the phage phi21 N peptide-boxB RNA complex Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination Selection of RRE RNA binding peptides using a kanamycin antitermination assay.Bacteriophage lambda N protein alone can induce transcription antitermination in vitro.RNA recognition by arginine-rich peptide motifs.RNA polymerase elongation factors Interaction between the phage HK022 Nun protein and the nut RNA of phage lambda Processive antitermination Transcription by moonlight: structural basis of an extraribosomal activity of ribosomal protein S10.HK022 Nun Requires Arginine-Rich Motif Residues Distinct from λ N.Escherichia coli NusA is required for efficient RNA binding by phage HK022 nun protein.Tethering of proteins to RNAs by bacteriophage proteins.Correction of mutations within the cystic fibrosis transmembrane conductance regulator by site-directed RNA editing An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch.Translational repression by a transcriptional elongation factor.Recognition modes of RNA tetraloops and tetraloop-like motifs by RNA-binding proteins.Binding of the bacteriophage P22 N-peptide to the boxB RNA motif studied by molecular dynamics simulations.Low energy CD of RNA hairpin unveils a loop conformation required for lambdaN antitermination activity.Putative intermediary stages for the molecular evolution from a ribozyme to a catalytic RNP.Learning from the Leaders: Gene Regulation by the Transcription Termination Factor Rho.Specific binding of Escherichia coli ribosomal protein S1 to boxA transcriptional antiterminator RNA.Design and development of a catalytic ribonucleoprotein.Bacteriophage P22 antitermination boxB sequence requirements are complex and overlap with those of lambda Role of Escherichia coli RNA polymerase alpha subunit in modulation of pausing, termination and anti-termination by the transcription elongation factor NusA.N protein from lambdoid phages transforms NusA into an antiterminator by modulating NusA-RNA polymerase flap domain interactions.The antitermination activity of bacteriophage lambda N protein is controlled by the kinetics of an RNA-looping-facilitated interaction with the transcription complex.Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE).The role of the T7 Gp2 inhibitor of host RNA polymerase in phage development A quantitative description of the binding states and in vitro function of antitermination protein N of bacteriophage lambda.The interaction surface of a bacterial transcription elongation factor required for complex formation with an antiterminator during transcription antitermination.A novel stable RNA pentaloop that interacts specifically with a motif peptide of lambda-N protein.A single spacer nucleotide determines the specificities of two mRNA regulatory proteins.The site of action of the antiterminator protein N from the lambdoid phage H-19B.Antitermination in bacteriophage λ

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P2860

Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda

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Proceedings of the National Academy of Sciences of the United States of America

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Bipartite function of a small ...... nation in bacteriophage lambda

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A Das

http://www.w3.org/2001/XMLSchema#string

J DeVito

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J Garcia-Mena

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K Wolska

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S Chattopadhyay

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P2860

DNA sequencing with chain-terminating inhibitors

A rapid alkaline extraction procedure for screening recombinant plasmid DNA

NusA protein is necessary and sufficient in vitro for phage lambda N gene product to suppress a rho-independent terminator placed downstream of nutL.

E. coli NusA protein binds in vitro to an RNA sequence immediately upstream of the boxA signal of bacteriophage lambda.

New models for the mechanism of transcription elongation and its regulation.

Effects of all single base substitutions in the loop of boxB on antitermination of transcription by bacteriophage lambda's N protein.

How the phage lambda N gene product suppresses transcription termination: communication of RNA polymerase with regulatory proteins mediated by signals in nascent RNA.

Control of transcription processivity in phage lambda: Nus factors strengthen the termination-resistant state of RNA polymerase induced by N antiterminator.

Mutations of the phage lambda nutL region that prevent the action of Nun, a site-specific transcription termination factor.

Action of an RNA site at a distance: role of the nut genetic signal in transcription antitermination by phage-lambda N gene product.

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