Lysine/RNA-interactions drive and regulate biomolecular condensation

Tina Ukmar-Godec, Saskia Hutten, Matthew P. Grieshop, Nasrollah Rezaei-Ghaleh, Maria-Sol Cima-Omori, Jacek Biernat, Eckhard Mandelkow, Johannes Söding, Dorothee Dormann and Markus Zweckstetter ()
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Tina Ukmar-Godec: University of Göttingen
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)
Johannes Söding: Max Planck Institute for Biophysical Chemistry
Dorothee Dormann: Ludwig-Maximilians−University Munich
Markus Zweckstetter: German Center for Neurodegenerative Diseases (DZNE)

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-10792-y

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