Depletion Interactions Modulate the Binding Between Disordered Proteins in Crowded Environments
Washington University School of Medicine Digital Commons@Becker Open Access Publications 2020 Depletion interactions modulate the binding between disordered proteins in crowded environments Franziska Zosel Andrea Soranno Karin J. Buholzer Daniel Nettels Benjamin Schuler Follow this and additional works at: https://digitalcommons.wustl.edu/open_access_pubs Depletion interactions modulate the binding between disordered proteins in crowded environments Franziska Zosela,1,2, Andrea Sorannoa,b,2, Karin J. Buholzera, Daniel Nettelsa, and Benjamin Schulera,c,2 aDepartment of Biochemistry, University of Zurich, 8057 Zurich, Switzerland; bDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO 63130; and cDepartment of Physics, University of Zurich, 8057 Zurich, Switzerland Edited by Martin Gruebele, University of Illinois at Urbana–Champaign, Urbana, IL, and approved April 7, 2020 (received for review December 14, 2019) Intrinsically disordered proteins (IDPs) abound in cellular regulation. effects on all these observables can be rationalized quantitatively Their interactions are often transitory and highly sensitive to salt within the framework of depletion interactions, the effective attractive concentration and posttranslational modifications. However, little force that arises between particles in a solution of solutes that are is known about the effect of macromolecular crowding on the preferentially excluded from the vicinity of the particles (37–39). interactions of IDPs with their cellular targets. Here, we investigate The depletion effects that cause the interaction between two the influence of crowding on the interaction between two IDPs that proteins in a crowded solution have the same entropic origin as fold upon binding, with polyethylene glycol as a crowding agent. those leading to the conformational collapse of IDPs in the Single-molecule spectroscopy allows us to quantify the effects of presence of crowding agents (20, 40).
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