Specificity of RNA-RNA helix recognition.
Functional RNAs often form compact structures characterized by closely packed helices. Crystallographic analysis of several large RNAs revealed a prevalent interaction in which unpaired adenosine residues dock into the minor groove of a receptor helix. This A-minor motif, potentially the most important element responsible for global RNA architecture, has also been suggested to contribute to the fidelity of protein synthesis by discriminating against near-cognate tRNAs on the ribosome. The specificity of A-minor interactions is fundamental to RNA tertiary structure formation, as well as to their proposed role in translational accuracy. To investigate A-minor motif specificity, we analyzed mutations in an A-minor interaction within the Tetrahymena group I self-splicing intron. Thermodynamic and x-ray crystallographic results show that the A-minor interaction strongly prefers canonical base pairs over base mismatches in the receptor helix, enabling RNA interhelical packing through specific recognition of Watson-Crick minor groove geometry.
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Daniel J
DJ
Battle
Jennifer A
JA
Doudna
D020029:Base Pairing; D018360:Crystallography, X-Ray; D009690:Nucleic Acid Conformation; D010957:Plasmids; D012313:RNA / Q000737:chemistry*
D012313:RNA