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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif.

We have dissected the protein and nucleic acid determinants that direct a group of transcriptional antiterminators to their specific target operons. These antiterminators, the N gene products of phages lambda, 21, and P22, function solely with their respective recognition sites, nut, to modify RNA polymerase to a termination-resistant form. We demonstrate that a unique hairpin sequence within each nut site, called boxB, confers genome specificity by interacting with a small amino-terminal domain of the cognate N protein. This interaction is dependent upon an arginine-rich subdomain, which is conserved not only among the N proteins but also in many RNA binding proteins from ribosomes and RNA virus capsids. Notably, this motif constitutes an essential domain of the HIV protein Tat whose function as a trans-activator requires a specific hairpin sequence.[1]

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