Interaction of protein SRP19 with signal recognition particle RNA lacking individual RNA-helices.
Derivatives of human SRP-RNA were constructed by site-directed mutagenesis and tested for their ability to interact with protein SRP19. An RNA missing helix 6 barely interacts with SRP19, while the helix 8-deletion mutant retains much binding capability. A mutant RNA consisting just of helix 6 also binds the protein, but not as well as the unaltered molecule. SRP19 interacts to a full extent with the fourth mutant RNA composed of helices 6, 7, 8 and a portion of helix 5. It is concluded that helix 6- and not helix 8- is the major SRP19 binding site. Helices 7, 8 and portions of helix 5 contribute to the formation of a functional site. These results agree with data suggesting a proximity of helix 6 and the conserved part of SRP-RNA.
Zwieb
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Department of Molecular Biology, University of Texas Health Center, Tyler 75710.
D001483:Base Sequence; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009690:Nucleic Acid Conformation; D010957:Plasmids; D012313:RNA / Q000235:genetics* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism*; D018271:Signal Recognition Particle; D013379:Substrate Specificity
D012261:Ribonucleoproteins; D018271:Signal Recognition Particle; D012313:RNA