Titel
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution
Autor*in
Tyler Mrozowich
Alberta RNA Research & Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge
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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.
Stichwort
Biophysical chemistryBiophysicsComputational biophysicsMolecular biophysicsRNA
Objekt-Typ
Sprache
Englisch [eng]
Persistent identifier
Erschienen in
Titel
Nature Communications
Band
11
Ausgabe
1
ISSN
2041-1723
Erscheinungsdatum
2020
Publication
Springer Science and Business Media LLC
Erscheinungsdatum
2020
Zugänglichkeit
Rechte
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