2008
DOI: 10.1128/jb.00059-08
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Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of λ

Abstract: Transcription antitermination in phages and P22 uses N proteins that bind to similar boxB RNA hairpins in regulated transcripts. In contrast to the 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 plasmidbased antitermination system to screen boxBs with random loops and to test boxB mutants. We fi… Show more

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Cited by 13 publications
(24 citation statements)
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“…We found that this residue can be mutated to similar residues capable of packing against Cyt9. P22 boxB can tolerate mutation of the extruded base at boxB position 9 with little loss of activity (11), and the role of Ile28 is most likely to recognize the 3-out GNRA-like loop conformation. Presumably, any residue with a hydrophobic face can play the same role.…”
Section: Resultsmentioning
confidence: 99%
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“…We found that this residue can be mutated to similar residues capable of packing against Cyt9. P22 boxB can tolerate mutation of the extruded base at boxB position 9 with little loss of activity (11), and the role of Ile28 is most likely to recognize the 3-out GNRA-like loop conformation. Presumably, any residue with a hydrophobic face can play the same role.…”
Section: Resultsmentioning
confidence: 99%
“…Available genetic (11,15), biochemical (2), and NMR (5, 9, 30, 37) evidence suggests that the P22, , and 21 N proteins recognize boxB conformation, with little direct recognition of RNA sequence. The roles of only a few P22 N residues in boxB recognition and specificity are well understood based on the available P22 N-boxB NMR data (5) and mutagenesis data (18).…”
Section: Resultsmentioning
confidence: 99%
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