Disordered RNA chaperones can enhance nucleic acid folding via local charge screening
| Autor: | Holmstrom, Erik D., Liu, Zhaowei, Nettels, Daniel, Best, Robert B., Schuler, Benjamin |
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| Přispěvatelé: | University of Zurich, Holmstrom, Erik D |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
RNA Folding
Science Static Electricity Biophysics 610 Medicine & health 1600 General Chemistry Genome Viral Hepacivirus Article Computational biophysics 1300 General Biochemistry Genetics and Molecular Biology Nucleic Acids 10019 Department of Biochemistry lcsh:Science Intrinsically disordered proteins Viral Core Proteins virus diseases Nucleocapsid Proteins Molecular biophysics Single Molecule Imaging 3100 General Physics and Astronomy Spectrometry Fluorescence RNA RNA Viral 570 Life sciences biology lcsh:Q Dimerization Molecular Chaperones |
| Zdroj: | Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. RNA chaperones, such as the hepatitic C virus (HCV) core protein, are proteins that aid in the folding of nucleic acids. Here authors use single‐molecule spectroscopy and simulation to show that the HCV core protein acts as a flexible macromolecular counterion which facilitates nucleic acid folding. |
| Databáze: | OpenAIRE |
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