Recognition of a tetranucleotide loop of signal recognition particle RNA by protein SRP19.
The interaction of protein SRP19 with the RNA component of human signal recognition particle (SRP) was studied by site-directed mutagenesis of the SRP RNA. The effects of nucleotide changes in the tetranucleotide loop (tetraloop) of helix 6 showed that SRP19 recognizes a tetraloop in a sequence-specific manner. Adenosine 149 at the third position of the tetraloop was essential for binding. In contrast, changes of the base at the second position had no effect. Mutations that disrupt or compensate individual SRP RNA helices were generated to investigate the importance of base pairing and to identify other binding sites. Considerable base pairing was essential in helix 6. Another SRP19-binding site was located in the distal part of helix 8. The primary sequences of the tetraloop-binding protein SR19 and of bacterial ribosomal protein S15 are shown to be similar.
Zwieb
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Department of Molecular Biology, University of Texas Health Science Center, Tyler 75710.
D000595:Amino Acid Sequence; D001482:Base Composition; D001483:Base Sequence; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides; D016133:Polymerase Chain Reaction; D011485:Protein Binding; D012313:RNA / Q000235:genetics* / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000235:genetics* / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D018271:Signal Recognition Particle
D009838:Oligodeoxyribonucleotides; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins; D018271:Signal Recognition Particle; D012313:RNA