The (un)structural biology of biomolecular liquid-liquid phase separation using NMR spectroscopy

Liquid-liquid phase separation (LLPS) of proteins and nucleic acids is a phenomenon that underlies membraneless compartmentalization of the cell. The underlying molecular interactions that underpin biomolecular LLPS have been of increased interest due to the importance of membraneless organelles in...

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Bibliographic Details
Published in:The Journal of biological chemistry 2020-02, Vol.295 (8), p.2375-2384
Main Authors: Murthy, Anastasia C., Fawzi, Nicolas L.
Format: Article
Language:English
Subjects:
heterogeneous nuclear ribonucleoprotein (hnRNP)
intrinsically disordered protein
Intrinsically Disordered Proteins - chemistry
JBC Reviews
liquid-liquid phase separation
Magnetic Resonance Spectroscopy
Motion
nuclear magnetic resonance (NMR)
Protein Conformation
protein-protein interaction
RNA-binding proteins
structural biology
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Summary:Liquid-liquid phase separation (LLPS) of proteins and nucleic acids is a phenomenon that underlies membraneless compartmentalization of the cell. The underlying molecular interactions that underpin biomolecular LLPS have been of increased interest due to the importance of membraneless organelles in facilitating various biological processes and the disease association of several of the proteins that mediate LLPS. Proteins that are able to undergo LLPS often contain intrinsically disordered regions and remain dynamic in solution. Solution-state NMR spectroscopy has emerged as a leading structural technique to characterize protein LLPS due to the variety and specificity of information that can be obtained about intrinsically disordered sequences. This review discusses practical aspects of studying LLPS by NMR, summarizes recent work on the molecular aspects of LLPS of various protein systems, and discusses future opportunities for characterizing the molecular details of LLPS to modulate phase separation.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.REV119.009847