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  Lysine/RNA-interactions drive and regulate biomolecular condensation.

Ukmar-Godec, T., Hutten, S., Grieshop, M. P., Rezaei-Ghaleh, N., Cima-Omori, M. O., Biernat, J., et al. (2019). Lysine/RNA-interactions drive and regulate biomolecular condensation. Nature Communications, 10(1): 2909. doi:10.1038/s41467-019-10792-y.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-F3C7-A Version Permalink: http://hdl.handle.net/21.11116/0000-0003-F3CB-6
Genre: Journal Article

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 Creators:
Ukmar-Godec, T., Author
Hutten, S., Author
Grieshop, M. P., Author
Rezaei-Ghaleh, N., Author
Cima-Omori, M. O., Author
Biernat, J., Author
Mandelkow, E., Author
Söding, J.1, Author              
Dormann, D., Author
Zweckstetter, M.2, Author              
Affiliations:
1Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 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.

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Language(s): eng - English
 Dates: 2019-07-02
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-019-10792-y
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Title: Nature Communications
Source Genre: Journal
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Pages: - Volume / Issue: 10 (1) Sequence Number: 2909 Start / End Page: - Identifier: -