ArticleProceedings of the National Academy of Sciences of the United States of America2003
Phage HK022 Nun protein represses translation of phage lambda N (transcription termination/translation repression).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 11 citations in OpenAlex.
- RNA polymerase elongation factors.Annual review of microbiology · 2008Review
- Role of an RNase III binding site in transcription termination at lambda nutL by HK022 Nun protein.Journal of bacteriology · 2006Article
- Transcription regulation mechanisms of bacteriophages: recent advances and future prospects.BioengineeredReview
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6 authors at 3 institutions in 1 country.
Funding
Abstract
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 translation of the lambda N gene. Thus HK022 excludes lambda both by terminating transcription on the phage chromosome and by preventing translation of the essential lambda N gene. Like N autoregulation, translation repression by Nun requires host RNaseIII deficiency (rnc) or a mutation in the RNaseIII processing site (rIII) located between NUTL and the beginning of the N coding sequence. Our data support the idea that Nun bound at NUTL causes steric interference with ribosome attachment to the nearby N coding sequence. Two models, Nun acting alone or in complex with host proteins, are discussed.
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