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Enzymatic control over coacervation
Open accessAbstract
The discovery of membraneless organelles (MLOs) formed by liquid-liquid phase separation raised many questions about the spatial organization of biomolecular processes in cells, but also offered a new tool to mimic cellular media. Since disordered and charged protein domains are often necessary for phase separation, coacervates can be used as models both to understand MLO regulation and to develop dynamic cellular-like compartments. A versatile way to turn passive coacervate droplets into active and dynamic compartments is by introducing enzymatic reactions that affect parameters relevant for complex coacervation, such as the charge and length of the components. However, these reactions strictly take place in a heterogeneous medium, and the complexity thereof is hardly addressed, making it difficult to achieve true control. In this chapter we help close this gap by describing two coacervate systems in which enzymatic reactions endow coacervate droplets with a dynamic character. We further highlight the technical challenges posed by the two-phase systems and strategies to overcome them.
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“HPLC measurements of PyK kinetics in the presence of coacervates32, which show that the effective kcat of PyK in a coacervate dispersion is the same as in a solution.”
From Active coacervate droplets are protocells that grow and resist Ostwald ripening (2021) · cites this paper as [32]
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Cites
Aumiller, W. M., Pir Cakmak, F., Davis, B. W., & Keating, C. D. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b02499 · Cited by 325
Hierarchical Self-Assembly of a Copolymer-Stabilized Coacervate Protocell
Mason, A. F., Buddingh’, B. C., Williams, D. S., & van Hest, J. C. M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b10846 · Cited by 309
Research works printed but not linked: 44
- Aumiller, 2015, Phosphorylation-mediated RNA/peptide complex coacervation as a model for intracellular liquid organelles, Nature Chemistry, 8, 129, 10.1038/nchem.2414 · DOI
- Banani, 2017, Biomolecular condensates: Organizers of cellular biochemistry, Nature Reviews Molecular Cell Biology, 18, 285, 10.1038/nrm.2017.7 · DOI
- Banerjee, 2017, Reentrant phase transition drives dynamic substructure formation in ribonucleoprotein droplets, Angewandte Chemie International Edition in English, 56, 11354, 10.1002/anie.201703191 · DOI
- Beljanski, 1996, De novo synthesis of DNA-like molecules by polynucleotide phosphorylase in vitro, Journal of Molecular Evolution, 42, 493, 10.1007/BF02352279 · DOI
- Berry, 2015, RNA transcription modulates phase transition-driven nuclear body assembly, Proceedings of the National Academy of Sciences of the United States of America, 112, E5237
- Brangwynne, 2009, Germline P granules are liquid droplets that localize by controlled dissolution/condensation, Science, 324, 1729, 10.1126/science.1172046 · DOI
- Brangwynne, 2015, Polymer physics of intracellular phase transitions, Nature Physics, 11, 899, 10.1038/nphys3532 · DOI
- Bungenberg de Jong, 1929, Coacervation (partial miscibility in colloid systems), Proceedings of the Royal Academy of Sciences at Amsterdam, 32, 849
- Case, 2019, Stoichiometry controls activity of phase-separated clusters of actin signaling proteins, Science, 363, 1093, 10.1126/science.aau6313 · DOI
- Davis, 2015, Colocalization and sequential enzyme activity in aqueous biphasic systems: Experiments and modeling, Biophysical Journal, 109, 2182, 10.1016/j.bpj.2015.09.020 · DOI
- Deshpande, 2019, Spatiotemporal control of coacervate formation within liposomes, Nature Communications, 10, 1800, 10.1038/s41467-019-09855-x · DOI
- Elbaum-Garfinkle, 2015, The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics, Proceedings of the National Academy of Sciences of the United States of America, 112, 7189, 10.1073/pnas.1504822112 · DOI · Paper page
- Feric, 2016, Coexisting liquid phases underlie nucleolar subcompartments, Cell, 165, 1686, 10.1016/j.cell.2016.04.047 · DOI
- Harmon, 2017, Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins, Elife, 6, 10.7554/eLife.30294 · DOI · Paper page
- Kaibara, 2000, pH-induced coacervation in complexes of bovine serum albumin and cationic polyelectrolytes, Biomacromolecules, 1, 100, 10.1021/bm990006k · DOI
- Koga, 2011, Peptide-nucleotide microdroplets as a step towards a membrane-free protocell model, Nature Chemistry, 3, 720, 10.1038/nchem.1110 · DOI · Paper page
- Li, 2012, Phase transitions in the assembly of multivalent signalling proteins, Nature, 483, 336, 10.1038/nature10879 · DOI
- Maharana, 2018, RNA buffers the phase separation behavior of prion-like RNA binding proteins, Science, 360, 918, 10.1126/science.aar7366 · DOI
- Marianelli, 2018, Impact of macromolecular crowding on RNA/spermine complex coacervation and oligonucleotide compartmentalization, Soft Matter, 14, 368, 10.1039/C7SM02146A · DOI
- Mitrea, 2018, Methods for physical characterization of phase-separated bodies and membrane-less organelles, Journal of Molecular Biology, 430, 4773, 10.1016/j.jmb.2018.07.006 · DOI
- Mitrea, 2016, Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA, eLife, 5, 10.7554/eLife.13571 · DOI
- Mitrea, 2018, Self-interaction of NPM1 modulates multiple mechanisms of liquid-liquid phase separation, Nature Communications, 9, 842, 10.1038/s41467-018-03255-3 · DOI
- Nakashima, 2018, Reversible generation of coacervate droplets in an enzymatic network, Soft Matter, 14, 361, 10.1039/C7SM01897E · DOI · Paper page
- Nakashima, 2019, Biomolecular chemistry in liquid phase separated compartments, Frontiers in Molecular Biosciences, 6, 21, 10.3389/fmolb.2019.00021 · DOI
- Nott, 2016, Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters, Nature Chemistry, 8, 569, 10.1038/nchem.2519 · DOI
- Nott, 2015, Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles, Molecular Cell, 57, 936, 10.1016/j.molcel.2015.01.013 · DOI · Paper page
- Overbeek, 1957, Phase separation in polyelectrolyte solutions. Theory of complex coacervation, Journal of Cellular and Comparative Physiology, 49, 7, 10.1002/jcp.1030490404 · DOI
- Perry, 2015, PRISM-based theory of complex coacervation: Excluded volume versus chain correlation, Macromolecules, 48, 5040, 10.1021/acs.macromol.5b01027 · DOI
- Qamar, 2018, FUS phase separation is modulated by a molecular chaperone and methylation of arginine cation-pi interactions, Cell, 173, 720, 10.1016/j.cell.2018.03.056 · DOI
- Quinn, 2015, How fluorescent labelling alters the solution behaviour of proteins, Physical Chemistry Chemical Physics, 17, 31177, 10.1039/C5CP04463D · DOI
- Rai, 2018, Kinase-controlled phase transition of membraneless organelles in mitosis, Nature, 559, 211, 10.1038/s41586-018-0279-8 · DOI
- Saito, 2019, Acetylation of intrinsically disordered regions regulates phase separation, Nature Chemical Biology, 15, 51, 10.1038/s41589-018-0180-7 · DOI
- Schuster, 2018, Controllable protein phase separation and modular recruitment to form responsive membraneless organelles, Nature Communications, 9, 2985, 10.1038/s41467-018-05403-1 · DOI
- Semenov, 2015, Rational design of functional and tunable oscillating enzymatic networks, Nature Chemistry, 7, 160, 10.1038/nchem.2142 · DOI · Paper page
- Shin, 2017, Liquid phase condensation in cell physiology and disease, Science, 357, 10.1126/science.aaf4382 · DOI
- Sokolova, 2013, Enhanced transcription rates in membrane-free protocells formed by coacervation of cell lysate, Proceedings of the National Academy of Sciences of the United States of America, 110, 11692, 10.1073/pnas.1222321110 · DOI
- Spoelstra, 2020, Non-spherical coacervate shapes in an enzyme driven active system, Langmuir, 36, 1956, 10.1021/acs.langmuir.9b02719 · DOI
- Spruijt, 2010, Binodal compositions of polyelectrolyte complexes, Macromolecules, 43, 6476, 10.1021/ma101031t · DOI
- Su, 2016, Phase separation of signaling molecules promotes T cell receptor signal transduction, Science, 352, 595, 10.1126/science.aad9964 · DOI
- Te Brinke, 2018, Dissipative adaptation in driven self-assembly leading to self-dividing fibrils, Nature Nanotechnology, 13, 849, 10.1038/s41565-018-0192-1 · DOI
- Wang, 2014, Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. elegans, Elife, 3, 10.7554/eLife.04591 · DOI
- Wei, 2017, Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles, Nature Chemistry, 9, 1118, 10.1038/nchem.2803 · DOI
- Yewdall, 2019, Physicochemical characterization of polymer-stabilized coacervate protocells, Chembiochem, 20, 2643, 10.1002/cbic.201900195 · DOI
- Zwicker, 2016, Growth and division of active droplets provides a model for protocells, Nature Physics, 13, 408, 10.1038/nphys3984 · DOI
Cited by
Sorted by citations
Active coacervate droplets are protocells that grow and resist Ostwald ripening
Nakashima, K. K., van Haren, M. H. I., André, A. A. M., Robu, I., & Spruijt, E. (2021) · Nature Communications · doi:10.1038/s41467-021-24111-x · Cited by 209
Self-citation
Metadata
- Authors
- Nakashima, K. K., André, A. A. M., & Spruijt, E.
- Affiliations
- Radboud University Nijmegen (NL)
- Corresponding author
- Evan Spruijt
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 2021
- Volume
- 646
- Pages
- 353-389
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W3044057848
- Cited by
- 20
- References
- 2
- Citations by year
- 2025: 3 · 2024: 5 · 2023: 2 · 2022: 6 · 2021: 2
- FWCI
- 4.05
- Type
- book chapter
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
- PubMed (publishedVersion)
- Radboud Repository (Radboud University) (submittedVersion)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- 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
- coacervation, biomolecular condensates, liquid-liquid phase separation, coacervate droplets, protein charge, protein length, two-phase systems
- MeSH terms
- Organelles
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