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Phase Transitions of Associative Biomacromolecules

  • Rohit V. Pappu*
    Rohit V. Pappu
    Department of Biomedical Engineering, Center for Biomolecular Condensates (CBC), Washington University in St. Louis, St. Louis, Missouri 63130, United States
    *Email: [email protected]
    More by Rohit V. Pappu
  • Samuel R. Cohen
    Samuel R. Cohen
    Department of Biomedical Engineering, Center for Biomolecular Condensates (CBC), Washington University in St. Louis, St. Louis, Missouri 63130, United States
    Center of Regenerative Medicine, Washington University in St. Louis, St. Louis, Missouri 63130, United States
    More by Samuel R. Cohen
  • Furqan Dar
    Furqan Dar
    Department of Biomedical Engineering, Center for Biomolecular Condensates (CBC), Washington University in St. Louis, St. Louis, Missouri 63130, United States
    More by Furqan Dar
  • Mina Farag
    Mina Farag
    Department of Biomedical Engineering, Center for Biomolecular Condensates (CBC), Washington University in St. Louis, St. Louis, Missouri 63130, United States
    More by Mina Farag
  • , and 
  • Mrityunjoy Kar
    Mrityunjoy Kar
    Max Planck Institute of Cell Biology and Genetics, 01307 Dresden, Germany
    More by Mrityunjoy Kar
Cite this: Chem. Rev. 2023, 123, 14, 8945–8987
Publication Date (Web):March 7, 2023
https://doi.org/10.1021/acs.chemrev.2c00814
Copyright © 2023 American Chemical Society

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    Abstract

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    Multivalent proteins and nucleic acids, collectively referred to as multivalent associative biomacromolecules, provide the driving forces for the formation and compositional regulation of biomolecular condensates. Here, we review the key concepts of phase transitions of aqueous solutions of associative biomacromolecules, specifically proteins that include folded domains and intrinsically disordered regions. The phase transitions of these systems come under the rubric of coupled associative and segregative transitions. The concepts underlying these processes are presented, and their relevance to biomolecular condensates is discussed.

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    Cited By

    This article is cited by 12 publications.

    1. Saumyak Mukherjee, Sashary Ramos, Simone Pezzotti, Abhishek Kalarikkal, Tobias M. Prass, Laura Galazzo, Dominik Gendreizig, Natercia Barbosa, Enrica Bordignon, Martina Havenith, Lars V. Schäfer. Entropy Tug-of-War Determines Solvent Effects in the Liquid–Liquid Phase Separation of a Globular Protein. The Journal of Physical Chemistry Letters 2024, 15 (15) , 4047-4055. https://doi.org/10.1021/acs.jpclett.3c03421
    2. Partha Sarathi Roy. Complex Coacervate-Based Materials for Biomedicine: Recent Advancements and Future Prospects. Industrial & Engineering Chemistry Research 2024, 63 (13) , 5414-5487. https://doi.org/10.1021/acs.iecr.3c03830
    3. Begoña Monterroso, William Margolin, Arnold J. Boersma, Germán Rivas, Bert Poolman, Silvia Zorrilla. Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions. Chemical Reviews 2024, 124 (4) , 1899-1949. https://doi.org/10.1021/acs.chemrev.3c00622
    4. Yumeng Zhang, Shanlong Li, Xiping Gong, Jianhan Chen. Toward Accurate Simulation of Coupling between Protein Secondary Structure and Phase Separation. Journal of the American Chemical Society 2024, 146 (1) , 342-357. https://doi.org/10.1021/jacs.3c09195
    5. Keegan A. Lorenz-Ochoa, Carlos R. Baiz. Ultrafast Spectroscopy Reveals Slow Water Dynamics in Biocondensates. Journal of the American Chemical Society 2023, 145 (50) , 27800-27809. https://doi.org/10.1021/jacs.3c10862
    6. Guoming Gao, Nils G. Walter. Critical Assessment of Condensate Boundaries in Dual-Color Single Particle Tracking. The Journal of Physical Chemistry B 2023, 127 (36) , 7694-7707. https://doi.org/10.1021/acs.jpcb.3c03776
    7. William M. Jacobs. Theory and Simulation of Multiphase Coexistence in Biomolecular Mixtures. Journal of Chemical Theory and Computation 2023, 19 (12) , 3429-3445. https://doi.org/10.1021/acs.jctc.3c00198
    8. Emile Alghoul, Jihane Basbous, Angelos Constantinou. Compartmentalization of the DNA damage response: Mechanisms and functions. DNA Repair 2023, 128 , 103524. https://doi.org/10.1016/j.dnarep.2023.103524
    9. Pin Yu Chew, Jerelle A. Joseph, Rosana Collepardo-Guevara, Aleks Reinhardt. Aromatic and arginine content drives multiphasic condensation of protein-RNA mixtures. Biophysical Journal 2023, 118 https://doi.org/10.1016/j.bpj.2023.06.024
    10. Mina Farag, Alex S. Holehouse, Xiangze Zeng, Rohit V. Pappu. FIREBALL: A tool to fit protein phase diagrams based on mean-field theories for polymer solutions. Biophysical Journal 2023, 122 (12) , 2396-2403. https://doi.org/10.1016/j.bpj.2023.05.007
    11. Min Kyung Shinn, Rohit V. Pappu. Soaping up transcriptional condensates. Developmental Cell 2023, 58 (11) , 915-916. https://doi.org/10.1016/j.devcel.2023.05.002
    12. Zeyu Shen, Bowen Jia, Yang Xu, Jonas Wessén, Tanmoy Pal, Hue Sun Chan, Shengwang Du, Mingjie Zhang. Biological condensates form percolated networks with molecular motion properties distinctly different from dilute solutions. eLife 2023, 12 https://doi.org/10.7554/eLife.81907

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