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Lysine/RNA-interactions drive and regulate biomolecular condensation

Author

Listed:
  • Tina Ukmar-Godec

    (University of Göttingen
    German Center for Neurodegenerative Diseases (DZNE))

  • Saskia Hutten

    (Ludwig-Maximilians−University Munich)

  • Matthew P. Grieshop

    (Max Planck Institute for Biophysical Chemistry)

  • Nasrollah Rezaei-Ghaleh

    (University of Göttingen)

  • Maria-Sol Cima-Omori

    (German Center for Neurodegenerative Diseases (DZNE))

  • Jacek Biernat

    (German Center for Neurodegenerative Diseases (DZNE))

  • Eckhard Mandelkow

    (German Center for Neurodegenerative Diseases (DZNE)
    CAESAR Research Center)

  • Johannes Söding

    (Max Planck Institute for Biophysical Chemistry)

  • Dorothee Dormann

    (Ludwig-Maximilians−University Munich
    Munich Cluster for Systems Neurology (SyNergy))

  • Markus Zweckstetter

    (German Center for Neurodegenerative Diseases (DZNE)
    Max Planck Institute for Biophysical Chemistry)

Abstract

Cells form and use biomolecular condensates to execute biochemical reactions. The molecular properties of non-membrane-bound condensates are directly connected to the amino acid content of disordered protein regions. Lysine plays an important role in cellular function, but little is known about its role in biomolecular condensation. Here we show that protein disorder is abundant in protein/RNA granules and lysine is enriched in disordered regions of proteins in P-bodies compared to the entire human disordered proteome. Lysine-rich polypeptides phase separate into lysine/RNA-coacervates that are more dynamic and differ at the molecular level from arginine/RNA-coacervates. Consistent with the ability of lysine to drive phase separation, lysine-rich variants of the Alzheimer’s disease-linked protein tau undergo coacervation with RNA in vitro and bind to stress granules in cells. Acetylation of lysine reverses liquid–liquid phase separation and reduces colocalization of tau with stress granules. Our study establishes lysine as an important regulator of cellular condensation.

Suggested Citation

  • Tina Ukmar-Godec & Saskia Hutten & Matthew P. Grieshop & Nasrollah Rezaei-Ghaleh & Maria-Sol Cima-Omori & Jacek Biernat & Eckhard Mandelkow & Johannes Söding & Dorothee Dormann & Markus Zweckstetter, 2019. "Lysine/RNA-interactions drive and regulate biomolecular condensation," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10792-y
    DOI: 10.1038/s41467-019-10792-y
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    Cited by:

    1. Giuseppe Sicoli & Daniel Sieme & Kerstin Overkamp & Mahdi Khalil & Robin Backer & Christian Griesinger & Dieter Willbold & Nasrollah Rezaei-Ghaleh, 2024. "Large dynamics of a phase separating arginine-glycine-rich domain revealed via nuclear and electron spins," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Chongrui Zhang & Xufei Liu & Jiang Gong & Qiang Zhao, 2023. "Liquid sculpture and curing of bio-inspired polyelectrolyte aqueous two-phase systems," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    3. Damian Wollny & Benjamin Vernot & Jie Wang & Maria Hondele & Aram Safrastyan & Franziska Aron & Julia Micheel & Zhisong He & Anthony Hyman & Karsten Weis & J. Gray Camp & T.‐Y. Dora Tang & Barbara Tre, 2022. "Characterization of RNA content in individual phase-separated coacervate microdroplets," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    4. Mofan Feng & Xiaoxi Wei & Xi Zheng & Liangjie Liu & Lin Lin & Manying Xia & Guang He & Yi Shi & Qing Lu, 2024. "Decoding Missense Variants by Incorporating Phase Separation via Machine Learning," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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