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Molecular recognition by the Candida albicans group I intron: Tertiary interactions with an imino GcntdotA pair facilitate binding of the 5' exon and lower the KM for guanosine

Molecular recognition by the Candida albicans group I intron: Tertiary interactions with an imino GcntdotA pair facilitate binding of the 5' exon and lower the KM for guanosine

Biochemistry 41(25): 8113-8119

A GcntdotA pair at position -5 in the P1 helix of the Candida albicans ribozyme contributes to tertiary binding of the 5' exon substrate (Disney, M. D., Haidaris, C. G., and Turner, D. H. (2001) Biochemistry 40, 6507-6519). Here, the G in the GcntdotA pair is replaced with inosine (I) in both semisynthetic ribozymes and oligonucleotide mimics of the internal guide sequence. Comparisons of oligonucleotide binding affinity for these and other sequences indicate that the GcntdotA pair is in an imino conformation where the exocyclic amine of G contributes apprx1.4 kcal/mol to tertiary interactions that help dock the ribozyme's P1 helix. Furthemore, replacement of the GcntdotA pair with a G-C pair produces less favorable interactions with the 2'-hydroxyl group at the -3 position and a less favorable KM for pG in a ribozyme-catalyzed transesterification reaction. These results are also consistent with the GcntdotA pair promoting docking of the P1 helix into the catalytic core. Evidently, tertiary interactions with the exocyclic amino group of a G in a single GcntdotA pair can increase the equilibrium constant for tertiary folding of RNA by roughly 10-fold at 37degreeC. Results with a GcntdotU or GcntdotG pair replacing the GcntdotA pair at the -5 position suggest similar tertiary interactions with these pairs.

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