| Autor: |
Heidenreich M; Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel., Georgeson JM; Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel., Locatelli E; Faculty of Physics, University of Vienna, Vienna, Austria., Rovigatti L; Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK. lorenzo.rovigatti@uniroma1.it.; Department of Physics, Sapienza Università di Roma, Rome, Italy. lorenzo.rovigatti@uniroma1.it., Nandi SK; Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.; TIFR Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research, Hyderabad, India., Steinberg A; Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel., Nadav Y; Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel., Shimoni E; Department of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel., Safran SA; Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel. sam.safran@weizmann.ac.il., Doye JPK; Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK. jonathan.doye@chem.ox.ac.uk., Levy ED; Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. emmanuel.Levy@weizmann.ac.il. |
| Abstrakt: |
Protein self-organization is a hallmark of biological systems. Although the physicochemical principles governing protein-protein interactions have long been known, the principles by which such nanoscale interactions generate diverse phenotypes of mesoscale assemblies, including phase-separated compartments, remain challenging to characterize. To illuminate such principles, we create a system of two proteins designed to interact and form mesh-like assemblies. We devise a new strategy to map high-resolution phase diagrams in living cells, which provide self-assembly signatures of this system. The structural modularity of the two protein components allows straightforward modification of their molecular properties, enabling us to characterize how interaction affinity impacts the phase diagram and material state of the assemblies in vivo. The phase diagrams and their dependence on interaction affinity were captured by theory and simulations, including out-of-equilibrium effects seen in growing cells. Finally, we find that cotranslational protein binding suffices to recruit a messenger RNA to the designed micron-scale structures. |
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