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Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
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Lysine/RNA-interactions drive and regulate biomolecular condensation
Tina Ukmar-Godec1,2, Saskia Hutten3, Matthew P Grieshop4
1Department of Neurology, University Medical Center Göttingen, University of Göttingen, Waldweg 33, 37073, Göttingen, Germany.
Nature Communications
|July 4, 2019
Summary
Lysine regulates cellular condensation by driving phase separation in biomolecular condensates. This amino acid
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Cells utilize biomolecular condensates for biochemical reactions.
- Disordered protein regions and amino acid content dictate condensate properties.
- The role of lysine in biomolecular condensation is largely unknown.
Purpose of the Study:
- Investigate lysine's role in the formation and properties of biomolecular condensates.
- Determine if lysine influences phase separation and condensate dynamics.
- Explore lysine's impact on cellular condensation processes.
Main Methods:
- Proteomic analysis of disordered regions in P-body proteins.
- In vitro phase separation assays with lysine-rich polypeptides and RNA.
- Biophysical characterization of lysine/RNA-coacervates versus arginine/RNA-coacervates.
- In vitro and cellular studies using lysine-rich tau variants and stress granules.
- Analysis of lysine acetylation's effect on phase separation and stress granule localization.
Main Results:
- Lysine is enriched in disordered protein regions within P-bodies.
- Lysine-rich polypeptides form dynamic lysine/RNA-coacervates, distinct from arginine/RNA-coacervates.
- Lysine drives RNA coacervation and stress granule binding for tau variants.
- Lysine acetylation inhibits phase separation and reduces tau's stress granule colocalization.
Conclusions:
- Lysine is a key regulator of cellular condensation.
- Lysine's enrichment in disordered regions influences condensate formation and dynamics.
- Modulating lysine acetylation offers a mechanism to control condensate properties and cellular localization.
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