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A guanosine-centric mechanism for RNA chaperone function
Jacob K Grohman1, Robert J Gorelick, Colin R Lickwar
1Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599-3290, USA.
Science (New York, N.Y.)
|March 9, 2013
Summary
RNA chaperones, like nucleocapsid (NC) protein, accelerate RNA folding by weakening guanosine interactions. This simplifies complex RNA folding pathways, revealing chaperone mechanisms.
Area of Science:
- Molecular Biology
- Biochemistry
- Structural Biology
Background:
- RNA chaperones are crucial for RNA structural formation and function.
- Understanding RNA chaperone mechanisms is vital for explaining RNA biogenesis and activity.
Purpose of the Study:
- To elucidate the mechanism by which RNA chaperones facilitate RNA folding.
- To investigate the role of specific nucleotide interactions in chaperone-mediated folding.
Main Methods:
- Time-resolved nucleotide-resolution analysis of retroviral RNA packaging domain dimerization.
- Comparative studies with and without nucleocapsid (NC) chaperone.
- Assessment of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) protein effects.
- RNA folding assays using guanosine-to-inosine substitutions.
Main Results:
- In the absence of chaperones, RNA dimerization involved multiple slow intermediates.
- Nucleocapsid (NC) chaperone and hnRNP A1 accelerated dimerization via a single intermediate.
- Both chaperones preferentially interacted with guanosine residues.
- Substitution of guanosine with inosine resulted in rapid folding without chaperones.
Conclusions:
- RNA chaperones simplify folding landscapes by weakening guanosine-mediated intramolecular interactions.
- This mechanism explains the diverse activities of RNA chaperones in RNA structural biogenesis.
- Guano-sine interactions are key targets for chaperone-assisted RNA folding.
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