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Article

Phage HK022 Nun protein represses translation of phage lambda N (transcription termination/translation repression).

Proceedings of the National Academy of Sciences of the United States of America - 29 Apr 2003

Kim Hyeong C, Zhou Jian-guang, Wilson Helen R, Mogilnitskiy Grigoriy, Court Donald L, Gottesman Max E

Abstract excerpt

The N-terminal arginine-rich motif of phage HK022 Nun protein binds to NUT sequences in phage lambda nascent transcripts and induces transcription termination. Interactions between the Nun C terminus and RNA polymerase as well as the DNA template are required for termination. We have isolated Nun C-terminal point and deletion mutants that are unable to block transcription. The mutants bind NUT RNA and inhibit...

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Identifiers

PMID: 12684530
DOI: 10.1073/pnas.0430995100
PMCID: PMC154341

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

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Phage HK022 Nun protein represses translation of phage lambda N (transcription termination/translation repression).PMID 12684530Read ↗

Use of a gene encoding a suppressor tRNA as a reporter of transcription: analyzing the action of the Nun protein of bacteriophage HK022.Semantic proximity Read ↗

Coliphage HK022 Nun protein inhibits RNA polymerase translocation.Semantic proximity Read ↗

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Lambda nutR mutations convert HK022 Nun protein from a transcription termination factor to a suppressor of termination.Semantic proximity Read ↗

Overexpression of phage HK022 Nun protein is toxic for Escherichia coli.Semantic proximity Read ↗

Translational repression by a transcriptional elongation factor.Semantic proximity Read ↗

Escherichia coli nusG mutations that block transcription termination by coliphage HK022 Nun protein.Semantic proximity Read ↗

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

The Y39A mutation of HK022 Nun disrupts a boxB interaction but preserves termination activity.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 ↗

Interactions of an Arg-rich region of transcription elongation protein NusA with NUT RNA: implications for the order of assembly of the lambda N antitermination complex in vivo.Semantic proximity Read ↗

A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein.Semantic proximity Read ↗

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