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Article

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

Genes & development - 1 Nov 1991

Nodwell J R, Greenblatt J

Abstract excerpt

The boxA and boxB components of the lambda nut site are important for transcriptional antitermination by the phage N protein. We show here that boxA and boxB RNA in N-modified transcription complexes are inaccessible to ribonucleases and have altered sensitivity to dimethylsulfate. N and NusA suffice to weakly protect boxB, independently of boxA and other factors. However, efficient protection of the entire nut...

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Source

Identifiers

PMID: 1834523
DOI: 10.1101/gad.5.11.2141

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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.

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The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.PMID 1834523Read ↗

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

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Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination.Semantic proximity Read ↗

Assembly of the N-dependent antitermination complex of phage lambda: NusA and RNA bind independently to different unfolded domains of the N protein.Semantic proximity Read ↗

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

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

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