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- W2089686095 abstract "To facilitate RNA-binding studies of the phage RB69 RegA translational repressor protein,regAwas configured to add six histidines to the carboxyl end of the protein.In vitrotranscription–translation from the T7 promoter on plasmid pSA1 yielded a RegA69-His6protein that binds nickel-Sepharose and elutes with 0.5 M imidazole. The system was further modified to avoid cloning and the toxic effects of RegA onEscherichia coliby the polymerase chain reaction (PCR), producing linear templates with the configuration T7 promoter-TIR-regA-His6. A translation initiation region was used that conforms to consensusE. coliand eukaryotic initiation sites and eliminates the target for RegA autogenous repression. RegA69-His6synthesized inE. coliS30 or wheat germ extracts displayed RNA-binding properties similar to wild-type RB69 RegA. Specificity of RNA binding was demonstrated byin vitrorepression of T4 gp44 and gp45 but not β-lactamase, by differential binding to poly(U)- and poly(C)-agarose, and by site-specific binding to a 23-base gene44target RNA but not to mutant44RNA. Therefore, addition of the His6tag to the C-terminus of RB69 RegA does not dramatically alter RNA binding, indicating that this region is not directly involved in site recognition. With access to several T4-like phage genomes andregAmutant sequences,in vitrosynthesis of His-tagged proteins directly from linear PCR products provides a convenient and efficient system to study RegA and other interesting RNA-binding proteins." @default.
- W2089686095 created "2016-06-24" @default.
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- W2089686095 date "1999-04-01" @default.
- W2089686095 modified "2023-10-16" @default.
- W2089686095 title "RNA-Binding Properties ofin VitroExpressed Histidine-Tagged RB69 RegA Translational Repressor Protein" @default.
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- W2089686095 doi "https://doi.org/10.1006/abio.1999.4025" @default.
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