4.8 Article

Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution

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NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -

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NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-13942-4

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  1. NIH NIGMS [GM110310]
  2. LANL LDRD
  3. NSERC
  4. LANL Institutional Computing

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Long non-coding RNAs (lncRNAs) constitute a significant fraction of the transcriptome, playing important roles in development and disease. However, our understanding of structure-function relationships for this emerging class of RNAs has been limited to secondary structures. Here, we report the 3-D atomistic structural study of epigenetic lncRNA, Braveheart (Bvht), and its complex with CNBP (Cellular Nucleic acid Binding Protein). Using small angle X-ray scattering (SAXS), we elucidate the ensemble of Bvht RNA conformations in solution, revealing that Bvht lncRNA has a well-defined, albeit flexible 3-D structure that is remodeled upon CNBP binding. Our study suggests that CNBP binding requires multiple domains of Bvht and the RHT/AGIL RNA motif. We show that RHT/AGIL, previously shown to interact with CNBP, contains a highly flexible loop surrounded by more ordered helices. As one of the largest RNA-only 3-D studies, the work lays the foundation for future structural studies of lncRNA-protein complexes.

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