| Literature DB >> 33469149 |
Joris Van Lindt1,2, Anna Bratek-Skicki3,4, Phuong N Nguyen1,2,5, Donya Pakravan6,7, Luis F Durán-Armenta1,2, Agnes Tantos8, Rita Pancsa8, Ludo Van Den Bosch6,7, Dominique Maes2, Peter Tompa9,10,11.
Abstract
Understanding the kinetics, thermodynamics, and molecular mechanisms of liquid-liquid phase separation (LLPS) is of paramount importance in cell biology, requiring reproducible methods for studying often severely aggregation-prone proteins. Frequently applied approaches for inducing LLPS, such as dilution of the protein from an urea-containing solution or cleavage of its fused solubility tag, often lead to very different kinetic behaviors. Here we demonstrate that at carefully selected pH values proteins such as the low-complexity domain of hnRNPA2, TDP-43, and NUP98, or the stress protein ERD14, can be kept in solution and their LLPS can then be induced by a jump to native pH. This approach represents a generic method for studying the full kinetic trajectory of LLPS under near native conditions that can be easily controlled, providing a platform for the characterization of physiologically relevant phase-separation behavior of diverse proteins.Entities:
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Year: 2021 PMID： 33469149 PMCID： PMC7815728 DOI： 10.1038/s42003-020-01596-8
Source DB: PubMed Journal: Commun Biol ISSN： 2399-3642