The solution structural ensembles of RNA kink-turn motifs and their protein complexes

Xuesong Shi (Lead / Corresponding author), Lin Huang, David M. J. Lilley, Pehr B. Harbury (Lead / Corresponding author), Daniel Herschlag (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)
    175 Downloads (Pure)

    Abstract

    With the growing number of crystal structures of RNA and RNA-protein complexes, a critical next step is understanding the dynamic solution behavior of these entities in terms of conformational ensembles and energy landscapes. To this end, we have used X-ray scattering interferometry (XSI) to probe the ubiquitous RNA kink-turn motif and its complexes with the canonical kink-turn binding protein L7Ae. XSI revealed that the folded kink-turn is best described as a restricted conformational ensemble. The ions present in solution alter the nature of this ensemble, and protein binding can perturb the kink-turn ensemble without collapsing it to a unique state. This study demonstrates how XSI can reveal structural and ensemble properties of RNAs and RNA-protein complexes and uncovers the behavior of an important RNA-protein motif. This type of information will be necessary to understand, predict and engineer the behavior and function of RNAs and their protein complexes.

    Original languageEnglish
    Pages (from-to)146-152
    Number of pages7
    JournalNature Chemical Biology
    Volume12
    Issue number3
    Early online date4 Jan 2016
    DOIs
    Publication statusPublished - Mar 2016

    Keywords

    • Base sequence
    • Interferometry
    • Molecular dynamics simulation
    • Molecular sequence data
    • Nucleic acid conformation
    • Nucleotide motifs
    • RNA
    • Scattering, Radiation
    • X-Rays
    • Journal article
    • Research support, N.I.H., Extramural
    • Research support, Non-U.S. Gov't

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