Unknown

Dataset Information

0

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains.

ABSTRACT: Prion-like domains (PLDs) can drive liquid-liquid phase separation (LLPS) in cells. Using an integrative biophysical approach that includes nuclear magnetic resonance spectroscopy, small-angle x-ray scattering, and multiscale simulations, we have uncovered sequence features that determine the overall phase behavior of PLDs. We show that the numbers (valence) of aromatic residues in PLDs determine the extent of temperature-dependent compaction of individual molecules in dilute solutions. The valence of aromatic residues also determines full binodals that quantify concentrations of PLDs within coexisting dilute and dense phases as a function of temperature. We also show that uniform patterning of aromatic residues is a sequence feature that promotes LLPS while inhibiting aggregation. Our findings lead to the development of a numerical stickers-and-spacers model that enables predictions of full binodals of PLDs from their sequences.

SUBMITTER: Martin EW 

PROVIDER: S-EPMC7297187 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains.

Martin Erik W EW   Holehouse Alex S AS   Peran Ivan I   Farag Mina M   Incicco J Jeremias JJ   Bremer Anne A   Grace Christy R CR   Soranno Andrea A   Pappu Rohit V RV   Mittag Tanja T  

Science (New York, N.Y.) 20200201 6478

Prion-like domains (PLDs) can drive liquid-liquid phase separation (LLPS) in cells. Using an integrative biophysical approach that includes nuclear magnetic resonance spectroscopy, small-angle x-ray scattering, and multiscale simulations, we have uncovered sequence features that determine the overall phase behavior of PLDs. We show that the numbers (valence) of aromatic residues in PLDs determine the extent of temperature-dependent compaction of individual molecules in dilute solutions. The vale  ...[more]

Similar Datasets

Unknown Clustering of Aromatic Residues in Prion-like Domains Can Tune the Formation, State, and Organization of Biomolecular Condensates.
| S-EPMC8638251 | biostudies-literature
Unknown Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior.
| S-EPMC3701498 | biostudies-literature
Unknown Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversity.
| S-EPMC4260602 | biostudies-literature
Unknown TET1 Interacts Directly with NANOG via Independent Domains Containing Hydrophobic and Aromatic Residues.
| S-EPMC7763487 | biostudies-literature
Unknown Phase behavior and critical activated dynamics of limited-valence DNA nanostars.
| S-EPMC3785745 | biostudies-literature
Unknown RNA-binding and prion domains: the Yin and Yang of phase separation.
| S-EPMC7515694 | biostudies-literature
Unknown Turing Patterning in Stratified Domains.
| S-EPMC7561598 | biostudies-literature
Unknown Prion-Like Domains in Phagobiota.
| S-EPMC5694896 | biostudies-literature
Unknown Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-like Phase Behavior.
| S-EPMC6086602 | biostudies-literature
Unknown Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains.
| S-EPMC5911940 | biostudies-literature