Zinc-finger protein CNBP alters the 3-D structure of IncRNA Braveheart in solution
dc.contributor.author | Kim, Doo N. | |
dc.contributor.author | Thiel, Bernhard C. | |
dc.contributor.author | Mrozowich, Tyler | |
dc.contributor.author | Hennelly, Scott P. | |
dc.contributor.author | Hofacker, Ivo L. | |
dc.contributor.author | Patel, Trushar R. | |
dc.contributor.author | Sanbonmatsu, Karissa Y. | |
dc.date.accessioned | 2024-06-19T21:44:22Z | |
dc.date.available | 2024-06-19T21:44:22Z | |
dc.date.issued | 2020 | |
dc.description | Open access article. Creative Commons Attribution 4.0 International license (CC BY 4.0) applies | |
dc.description.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. | |
dc.identifier.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 | |
dc.identifier.uri | https://hdl.handle.net/10133/6790 | |
dc.language.iso | en | |
dc.publisher | Nature Portfolio | |
dc.publisher.department | Department of Chemistry and Biochemistry | |
dc.publisher.faculty | Arts and Science | |
dc.publisher.institution | Los Alamos National Laboratory | |
dc.publisher.institution | University of Vienna | |
dc.publisher.institution | University of Lethbridge | |
dc.publisher.institution | New Mexico Consortium | |
dc.publisher.institution | University of Calgary | |
dc.publisher.institution | University of Alberta | |
dc.subject | Biophysical chemistry | |
dc.subject | Biophysics | |
dc.subject | Computational biophysics | |
dc.subject | Molecular biophysics | |
dc.subject | RNA | |
dc.subject | IncRNA | |
dc.subject | 3-D studies | |
dc.subject.lcsh | Protein complexes | |
dc.title | Zinc-finger protein CNBP alters the 3-D structure of IncRNA Braveheart in solution | |
dc.type | Article |