Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

N protein from lambdoid phages transforms NusA into an antiterminator by modulating NusA-RNA polymerase flap domain interactions.

Nucleic acids research - 13 Jul 2015

Mishra Saurabh, Sen Ranjan

Abstract excerpt

Interaction of the lambdoid phage N protein with the bacterial transcription elongation factor NusA is the key component in the process of transcription antitermination. A convex surface of E. coli NusA-NTD, located opposite to its RNA polymerase-binding domain (the β-flap domain), directly interacts with N in the antitermination complex. We hypothesized that this N-NusA interaction induces allosteric effects on...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacteriophages
Share to DNA-Directed RNA Polymerases
Share to Peptide Elongation Factors

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Interaction Domains and Motifs

Share to RNA-Binding Proteins

Share to Transcriptional Elongation Factors

Share to Viral Regulatory and Accessory Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 25990722
DOI: 10.1093/nar/gkv479
PMCID: PMC4499122

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

N protein from lambdoid phages transforms NusA into an antiterminator by modulating NusA-RNA polymerase flap domain interactions.PMID 25990722Read ↗

The interaction surface of a bacterial transcription elongation factor required for complex formation with an antiterminator during transcription antitermination.Semantic proximity Read ↗

Escherichia coli RNA polymerase mutations located near the upstream edge of an RNA:DNA hybrid and the beginning of the RNA-exit channel are defective for transcription antitermination by the N protein from lambdoid phage H-19B.Semantic proximity Read ↗

The alpha subunit of RNA polymerase and transcription antitermination.Semantic proximity Read ↗

Compromised factor-dependent transcription termination in a nusA mutant of Escherichia coli: spectrum of termination efficiencies generated by perturbations of Rho, NusG, NusA, and H-NS family proteins.Semantic proximity Read ↗

The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA.Semantic proximity Read ↗

RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.Semantic proximity Read ↗

The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.Semantic proximity Read ↗

Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins.Semantic proximity Read ↗

Transcription Elongation Factor NusA Is a General Antagonist of Rho-dependent Termination in Escherichia coli.Semantic proximity Read ↗

Effect of Escherichia coli nusG function on lambda N-mediated transcription antitermination.Semantic proximity Read ↗

Bacteriophage lambda N-dependent transcription antitermination. Competition for an RNA site may regulate antitermination.Semantic proximity Read ↗

Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.