RNA conformational propensities determine cellular activity
M. L. Kelly, R. Roy, A. Geng, L. R. Ganser, A. Manghrani, B. R. Cullen, U. Schulze-Gahmen, D. Herschlag, H. M. Al-Hashimi
Abstract
Cellular processes are the product of interactions between biomolecules, which associate to form biologically active complexes 1. These interactions are mediated by intermolecular contacts, which if disrupted, lead to alterations in cell physiology. Nevertheless, the formation of intermolecular contacts nearly universally requires changes in the conformations of the interacting biomolecules. As a result, binding affinity and cellular activity crucially depend not only on the strength of the contacts, but also on the inherent propensities to form binding-competent conformational states2,3. Thus, conformational penalties are ubiquitous in biology and must be known in order to quantitatively model binding energetics for protein and nucleic acid interactions4,5. However, conceptual and technological limitations have hindered our ability to dissect and quantitatively measure how conformational propensities impact cellular activity. Here, we systematically altered and determined the propensities for forming the protein-bound conformation of HIV-1 TAR RNA. These propensities quantitatively predicted the binding affinities of TAR to the RNA-binding region of the Tat protein and predicted the extent of HIV-1 Tat-dependent transactivation in cells. Our results establish the role of ensemble-based conformational propensities in cellular activity and reveal an example of a cellular process driven by an exceptionally rare and short-lived RNA conformational state.
02 /Specification & Classification
Click any tag to browse matching papersReproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Integrative Ensemble Modeling reveals RNA conformations targetable by small molecules
Stefano Bosio, Vincent Schnapka, … Matteo Masetti·bioRxiv·Jul 29, 2026
- Probing RNA conformational equilibria within the functional cellular context
L. R. Ganser, C.-C. Chu, … H. M. Al-Hashimi·bioRxiv·Sep 1, 2019
- Conformational and Environmental Determinants of RNA Solvation Dynamics: Roles of Intrinsic Flexibility, Allostery, and Protein Binding
Amrita Chakraborty, Susmita Roy·Physical Chemistry Chemical PhysicsPeer-reviewed·Jan 1, 2026
- The HIV-1 Integrase C-Terminal domain induces TAR RNA structural changes promoting Tat binding.
C. Rocchi, C. Louvat, … F. Fiorini·bioRxiv·Oct 21, 2021
- Nonequilibrium phases of a biomolecular condensate facilitated by enzyme activity
Sebastian Coupe, Nikta Fakhri·Soft MatterPeer-reviewed·Jan 1, 2026
- Dynamic ensemble of HIV-1 RRE stem IIB reveals non-native conformations that disrupt the Rev binding site
C.-C. Chu, R. Plangger, … H. M. Al-Hashimi·bioRxiv·Dec 18, 2018