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Disordered RNA chaperones can enhance nucleic acid folding via local charge screening
Holmstrom, Erik D. Liu, Zhaowei Nettels, Daniel Best, Robert B. Schuler, Benjamin
Holmstrom, Erik D.
Liu, Zhaowei
Nettels, Daniel
Best, Robert B.
Schuler, Benjamin
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Abstract
RNA chaperones are proteins that aid in the folding of nucleic acids, but remarkably, many of these proteins are intrinsically disordered. How can these proteins function without a well-defined three-dimensional structure? Here, we address this question by studying the hepatitis C virus core protein, a chaperone that promotes viral genome dimerization. Using single-molecule fluorescence spectroscopy, we find that this positively charged disordered protein facilitates the formation of compact nucleic acid conformations by acting as a flexible macromolecular counterion that locally screens repulsive electrostatic interactions with an efficiency equivalent to molar salt concentrations. The resulting compaction can bias unfolded nucleic acids towards folding, resulting in faster folding kinetics. This potentially widespread mechanism is supported by molecular simulations that rationalize the experimental findings by describing the chaperone as an unstructured polyelectrolyte.
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This work is licensed under a Creative Commons Attribution 4.0 International License.
Date
2019-06-05
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Nature Research
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Keywords
RNA, Biophysics, Computational biophysics, Intrinsically disordered proteins, Molecular biophysics
Citation
Holmstrom, E. D., Liu, Z., Nettels, D., Best, R. B., & Schuler, B. (2019). Disordered RNA chaperones can enhance nucleic acid folding via local charge screening. Nature communications, 10(1), 2453. https://doi.org/10.1038/s41467-019-10356-0