Relationship of sequence and phase separation in protein low-complexity regions

Martin, Erik W.; Mittag, Tanja

doi:10.1021/acs.biochem.8b00008

Cited by 389RNA Research and SplicingProtein Structure and DynamicsRNA and protein synthesis mechanisms

Relationship of sequence and phase separation in protein low-complexity regions

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Martin, Erik W., Mittag, Tanja·2018·Biochemistry

DOI 10.1021/acs.biochem.8b00008PMC PMC6476794

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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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Many proteins with low complexity prion-like domains (PLDs) are drivers of phase separation.
“Many proteins with low complexity prion-like domains (PLDs) are drivers of phase separation.87”
From AlphaFold and Implications for Intrinsically Disordered Proteins (2021) · cites this paper as [87]

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Authors: Martin, E. W., & Mittag, T.
Affiliations: St. Jude Children's Research Hospital (US)
Corresponding author: Martin, Erik W.
Mittag, Tanja
ORCID: Martin, Erik W.
Mittag, Tanja
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2018-03-08
Volume: 57
Issue: 17
Pages: 2478-2487
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/acs.biochem.8b00008
PMC: PMC6476794
OpenAlex: W2792129356
Cited by: 389
References: 67
Citations by year: 2026: 35 · 2025: 53 · 2024: 65 · 2023: 44 · 2022: 45 · 2021: 66 · 2020: 36 · 2019: 38 · 2018: 7
FWCI: 13.00
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: St. Jude Children's Research Hospital
National Institute of General Medical Sciences (R01 GM112846)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: low complexity regions, liquid-liquid phase separation, biomolecular condensates, polymer physics, cell compartmentalization, stress response, miscibility, protein sequence classification
MeSH terms: Protein Domains, Amino Acids, Cell Compartmentation, Hydrogen-Ion Concentration, Proteins, Temperature, Thermodynamics, Phase Transition

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Relationship of sequence and phase separation in protein low-complexity regions

Abstract

Integrity signals

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