Abstract：
:Liquid-liquid phase separation is increasingly recognized as a process involved in cellular organization. Thus far, a detailed structural characterization of this intrinsically heterogeneous process has been challenging. Here we combine solid- and solution-state NMR spectroscopy to obtain atomic-level insights into the assembly and maturation of cytoplasmic processing bodies that contain mRNA as well as enzymes involved in mRNA degradation. In detail, we have studied the enhancer of decapping 3 (Edc3) protein that is a central hub for processing body formation in yeast. Our results reveal that Edc3 domains exhibit diverse levels of structural organization and dynamics after liquid-liquid phase separation. In addition, we find that interactions between the different Edc3 domains and between Edc3 and RNA in solution are largely preserved in the condensed protein state, allowing processing bodies to rapidly form and dissociate upon small alterations in the cellular environment.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Damman R,Schütz S,Luo Y,Weingarth M,Sprangers R,Baldus Mdoi
10.1038/s41467-019-12402-3subject
Has Abstractpub_date
2019-10-04 00:00:00pages
4536issue
1issn
2041-1723pii
10.1038/s41467-019-12402-3journal_volume
10pub_type
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