Zinc-finger protein CNBP alters the 3-D structure of IncRNA Braveheart in solution
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Date
2020
Authors
Kim, Doo N.
Thiel, Bernhard C.
Mrozowich, Tyler
Hennelly, Scott P.
Hofacker, Ivo L.
Patel, Trushar R.
Sanbonmatsu, Karissa Y.
Journal Title
Journal ISSN
Volume Title
Publisher
Nature Portfolio
Abstract
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.
Description
Open access article. Creative Commons Attribution 4.0 International license (CC BY 4.0) applies
Keywords
Biophysical chemistry , Biophysics , Computational biophysics , Molecular biophysics , RNA , IncRNA , 3-D studies
Citation
Kim, D. N., Thiel, B. C., Mrozowich, T., Hennelly, S. P., Hofacker, I. L., Patel, T. R., & Sanbonmatsu, K. Y. (2020). Zinc-finger protein CNBP alters the 3-D structure of IncRNA Braveheart in solution. Nature Communications, 11, Article 148. https://doi.org/10.1038/s41467-019-13942-4