Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome
Wanes, G.; Mohanty, U.; Whitford, P. C.
Show abstract
While it is known that ions are required for folding of RNA, little is known about how transient/probabilistic ionic interactions facilitate biologically-relevant conformational rearrangements. To address this, we developed a theoretical model that employs all-atom resolution, with a simplified representation of biomolecular energetics, explicit electrostatics and ions (K+, Cl-, Mg2+). For well-studied RNA systems (58-mer and Ade riboswitch), the model accurately describes the concentration-dependent ionic environment, including (bidentate) chelated and hydrated (diffuse/outer-shell) ions. With this foundation, we applied the model to simulate the yeast ribosome and quantified the ion-dependent energy landscape of intersubunit rotation. These calculations show how the energetics of rotation responds to millimolar changes in [MgCl2], which shift the distribution between rotation states and alter the kinetics by more than an order of magnitude. We find that this response to the ionic concentration correlates with formation and breakage of ion-mediated interactions (inner-shell and outer-shell) between the ribosomal subunits. This analysis provides a physical basis for understanding how transient ion-mediated interactions can regulate a large-scale biological process.
Matching journals
The top 4 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Metal Ion Sensing by Tetraloop-Like RNA Fragment: Role of Compact Intermediates with Non-Native Metal Ion-RNA Inner Shell Contacts 98%
- Dimerization Mechanism of HIV-1 RNA Hairpins to Extended Duplex Structures 97%
- Analysis of the dynamics of a complex, multipathway reaction: Insulin dimer dissociation 97%
Similar papers in this journal
- Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model 97%
- Prediction of phase separation propensities of disordered proteins from sequence 96%
- Fast calculation of small-angle scattering profiles of dense protein solutions modeled at the all-atom level 96%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.