Literature DB >> 33503539

The role of liquid-liquid phase separation in regulating enzyme activity.

Brian G O'Flynn1, Tanja Mittag2.   

Abstract

Liquid-liquid phase separation (LLPS) is now recognized as a common mechanism underlying regulation of enzyme activity in cells. Insights from studies in cells are complemented by in vitro studies aimed at developing a better understanding of mechanisms underlying such control. These mechanisms are often based on the influence of LLPS on the physicochemical properties of the enzyme's environment. Biochemical mechanisms underlying such regulation include the potential for concentrating reactants together, tuning reaction rates, and controlling competing metabolic pathways. LLPS is thus a powerful tool with extensive utilities at the cell's disposal, e.g. for consolidating cell survival under stress or rerouting metabolic pathways in response to the energy state of the cell. Here, we examin the evidence for how LLPS affects enzyme catalysis and begin to understand emerging concepts and expand our understanding of enzyme catalysis in living cells.
Copyright © 2021 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Biomolecular condensate; Catalysis; Crowding; Membraneless organelles; Metabolism; Stress response

Mesh:

Year:  2021        PMID: 33503539      PMCID: PMC8058252          DOI: 10.1016/j.ceb.2020.12.012

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  75 in total

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2.  A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

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3.  Enzymatic degradation of liquid droplets of DNA is modulated near the phase boundary.

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6.  Formation of Multiphase Complex Coacervates and Partitioning of Biomolecules within them.

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Journal:  Biomacromolecules       Date:  2019-11-27       Impact factor: 6.988

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Authors:  Michael Dzuricky; Bradley A Rogers; Abdulla Shahid; Paul S Cremer; Ashutosh Chilkoti
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  14 in total

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Review 4.  Merging Established Mechanisms with New Insights: Condensates, Hubs, and the Regulation of RNA Polymerase II Transcription.

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5.  The role of stress-activated RNA-protein granules in surviving adversity.

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7.  The HIV-1 Nucleocapsid Regulates Its Own Condensation by Phase-Separated Activity-Enhancing Sequestration of the Viral Protease during Maturation.

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8.  Spatiotemporal Dynamic Assembly/Disassembly of Organelle-Mimics Based on Intrinsically Disordered Protein-Polymer Conjugates.

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9.  RNA chain length and stoichiometry govern surface tension and stability of protein-RNA condensates.

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Review 10.  Higher-order organization of biomolecular condensates.

Authors:  Charlotte M Fare; Alexis Villani; Lauren E Drake; James Shorter
Journal:  Open Biol       Date:  2021-06-16       Impact factor: 6.411

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