Induced fit of RNA on binding the L7Ae protein to the kink-turn motif

Ben Turner, Sonya E. Melcher, Timothy J. Wilson, David G. Norman, David M.J. Lilley (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    99 Citations (Scopus)


    The kink-turn is a widespread motif in RNA consisting of a three-nucleotide bulge flanked on one side by consecutive A·G mismatches. Important examples are found in the ribosome, U4 RNA, and in snoRNAs involved in RNA modification. The motif is a common protein binding site, and the RNA has been found to adopt a tightly kinked conformation in crystal structures. However, in free solution there is a dynamic exchange between kinked and extended conformations, with the equilibrium driven toward the kinked form by the addition of metal ions. Here we used fluorescence resonance energy transfer (FRET) to show that the L7Ae protein of Archaeoglobus fulgidus binds to RNA containing a kink-turn with nanomolar affinity, and induces folding into the tightly kinked conformation even in the absence of metal ions. Thus this RNA may act as a relatively flexible hinge during RNA folding, until fixed into its ultimate kinked structure by the binding of L7 or related protein.

    Original languageEnglish
    Pages (from-to)1192-1200
    Number of pages9
    Issue number8
    Publication statusPublished - Aug 2005


    • K-turn
    • RNA structure
    • RNA-protein interaction

    ASJC Scopus subject areas

    • Molecular Biology


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