ArticleJournal of bacteriology2008
Bacteriophage P22 antitermination boxB sequence requirements are complex and overlap with those of lambda.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Early antitermination in the atypical coliphage mEp021 mediated by the Gp17 protein.Archives of virology · 2023Article
- Pull-down of Biotinylated RNA and Associated Proteins.Bio-protocol · 2022Article
- Genome analysis of Salmonella enterica serovar Typhimurium bacteriophage L, indicator for StySA (StyLT2III) restriction-modification system action.G3 (Bethesda, Md.) · 2021Article
- Global pairwise RNA interaction landscapes reveal core features of protein recognition.Nature communications · 2018Article
- HK022 Nun Requires Arginine-Rich Motif Residues Distinct from λ N.Journal of bacteriology · 2015Article
- Binding of the bacteriophage P22 N-peptide to the boxB RNA motif studied by molecular dynamics simulations.Biophysical journal · 2009Article
- The RNA-binding domain of bacteriophage P22 N protein is highly mutable, and a single mutation relaxes specificity toward lambda.Journal of bacteriology · 2008Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription antitermination in phages lambda and P22 uses N proteins that bind to similar boxB RNA hairpins in regulated transcripts. In contrast to the lambda N-boxB interaction, the P22 N-boxB interaction has not been extensively studied. A nuclear magnetic resonance structure of the P22 N peptide boxB(left) complex and limited mutagenesis have been reported but do not reveal a consensus sequence for boxB. We have used a plasmid-based antitermination system to screen boxBs with random loops and to test boxB mutants. We find that P22 N requires boxB to have a GNRA-like loop with no simple requirements on the remaining sequences in the loop or stem. U:A or A:U base pairs are strongly preferred adjacent to the loop and appear to modulate N binding in cooperation with the loop and distal stem. A few GNRA-like hexaloops have moderate activity. Some boxB mutants bind P22 and lambda N, indicating that the requirements imposed on boxB by P22 N overlap those imposed by lambda N. Point mutations can dramatically alter boxB specificity between P22 and lambda N. A boxB specific for P22 N can be mutated to lambda N specificity by a series of single mutations via a bifunctional intermediate, as predicted by neutral theories of evolution.
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Registered trials
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