A number of dynamic, protein-rich intracellular structures containing phase separated, unstructured proteins comprising low-complexity amino acid sequences have recently been shown to serve a variety of important cellular functions, including signaling, compartmentalization and stabilization. The understanding of these structures, and the ability to synthesize models of them, has been limited. Here we present simple methods for programming diverse assemblies comprised of a series of elastin-like polypeptides, model intrinsically disordered proteins possessing sequences of low-complexity. By encoding the stimulus-induced phase behavior of proteins at the amino acid sequence level, we demonstrate the reversible formation of a variety of protein-rich structures within microdroplets, ranging from uniform nano-, meso-, and micro-scale puncta (small, distinct particulates) to multilayered, orthogonally-phase-separated, multicomponent granules. The ability to build such protein assemblies can facilitate new insights into (1) the genetic to molecular to microscale relationships of phase separating proteins and their assembly, (2) the role of such granules in cell biology, and (3) engineering protein-based microgels.

Programming molecular self-assembly of intrinsically disordered proteins

251st National Meeting (2016)

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