Molecular interactions underlying liquid−liquid phase separation of the FUS low-complexity domain

The low-complexity domain of the RNA-binding protein FUS (FUS LC) mediates liquid−liquid phase separation (LLPS), but the interactions between the repetitive SYGQ-rich sequence of FUS LC that stabilize the liquid phase are not known in detail. By combining NMR and Raman spectroscopy, mutagenesis, an...

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Veröffentlicht in:	Nature structural & molecular biology 2019-07, Vol.26 (7), p.637-648
Hauptverfasser:	Murthy, Anastasia C., Dignon, Gregory L., Kan, Yelena, Zerze, Gül H., Parekh, Sapun H., Mittal, Jeetain, Fawzi, Nicolas L.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/535/878 631/45/535/878/1263 631/57/2269 BASIC BIOLOGICAL SCIENCES Biochemistry Biological Microscopy Biomedical and Life Sciences Chemical properties Compartmental analysis (Biology) Complexity Composition Computer simulation Engineering FUS protein Glutamine Health aspects Heterogeneity Humans Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Hydrophobicity Intrinsically disordered proteins Intrinsically Disordered Proteins - chemistry Life Sciences Liquid phases Macromolecules Membrane Biology Models, Molecular Molecular biology Molecular interactions Mutagenesis NMR NMR spectroscopy Nuclear magnetic resonance Phase separation Phase transformations (Statistical physics) Phase Transition Polypeptides Protein Conformation Protein Domains Protein research Protein Structure Protein Structure, Secondary Proteins Raman spectroscopy Residues Ribonucleic acid RNA RNA polymerase RNA-binding protein RNA-Binding Protein FUS - chemistry Secondary structure solution-state NMR Spectrum analysis Transcription factors Tyrosine
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