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Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions. | LitMetric

Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions.

Biochemistry

Department of Structural Biology , St. Jude Children's Research Hospital, Memphis , Tennessee 38105-3678 , United States.

Published: May 2018

AI Article Synopsis

  • * These proteins can phase separate in test conditions changed by factors like temperature and pH, which suggests they could help cells respond to stress.
  • * The study aims to improve understanding of how the amino acid composition in these low-complexity regions affects phase behavior, classifying them based on their properties to connect their sequences to biological processes.

Article Abstract

Liquid-liquid phase separation seems to play critical roles in the compartmentalization of cells through the formation of biomolecular condensates. Many proteins with low-complexity regions are found in these condensates, and they can undergo phase separation in vitro in response to changes in temperature, pH, and ion concentration. Low-complexity regions are thus likely important players in mediating compartmentalization in response to stress. However, how the phase behavior is encoded in their amino acid composition and patterning is only poorly understood. We discuss here that polymer physics provides a powerful framework for our understanding of the thermodynamics of mixing and demixing and for how the phase behavior is encoded in the primary sequence. We propose to classify low-complexity regions further into subcategories based on their sequence properties and phase behavior. Ongoing research promises to improve our ability to link the primary sequence of low-complexity regions to their phase behavior as well as the emerging miscibility and material properties of the resulting biomolecular condensates, providing mechanistic insight into this fundamental biological process across length scales.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6476794PMC
http://dx.doi.org/10.1021/acs.biochem.8b00008DOI Listing

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