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BP: Fachverband Biologische Physik

BP 3: Computational Biophysics I

BP 3.12: Vortrag

Montag, 17. März 2025, 12:45–13:00, H44

Co-translational (polysome-protein) condensation — •Zhouyi He, Jens-Uwe Sommer, and Tyler Harmon — Leibniz Institute of Polymer Research , 01069, Dresden, Germany

Biomolecular condensates are ubiquitous in cells and play crucial roles in cellular regulation. These condensates typically form via liquid-liquid phase separation, where protein-protein interactions are crucial. However, how condensates interact with protein translation machinery is poorly studied. During translation, multiple ribosomes are simultaneously translating each mRNA forming a poly-ribosome structure (polysome), which resembles beads packed on a string. On one end of the mRNA, the ribosomes have only extruded the start of the nascent protein, and on the other end the ribosomes have a nearly finished protein. Nascent proteins from translating polysomes can interact with the finished proteins that make up the condensate (co-translational condensation). Using coarse-grained simulations, we show that the architecture of encoded proteins determines whether the polysome is adsorbed to the condensate surface or remains in the cytoplasm. Furthermore, we employ a reaction-diffusion model to analyze the time scales relevant to this process. Additionally, we model the potential cellular advantages of this phenomenon, including enhanced cellular response times, reduced noise in protein concentration, and facilitation of post-translational modifications. This work establishes a theoretical framework for co-translational condensation and highlights new functions for condensates in cells and offers promising directions for experimental validation.

Keywords: Biomolecular condensates; Co-translational condensation; Reaction-diffusion model; Coarse-grained simulation; Polysome