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High-throughput Screening for Protein-based Inheritance in S. cerevisiae

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Published on: August 8, 2017

Decoding phase separation of prion-like domains through data-driven scaling laws.

M Julia Maristany¹, Anne Aguirre Gonzalez², Jorge R Espinosa³

¹Department of Physics, University of Cambridge, Cambridge, United Kingdom.

|February 12, 2025

Summary

Amino acid mutations in prion-like low complexity domains (PLDs) can alter biomolecular condensate stability. We found scaling laws predicting these changes, aiding in understanding protein behavior.

Keywords:

biomolecular condensates critical temperature disordered proteins none phase separation physics of living systems prion-like low complexity domains scaling laws

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Area of Science:

Biophysics
Molecular Biology
Protein Chemistry

Background:

Proteins with prion-like low complexity domains (PLDs) drive biomolecular condensate formation.
Amino acid mutations can disrupt PLD function and lead to misregulation.

Purpose of the Study:

To quantify the impact of amino acid mutations on the stability of PLDs.
To identify predictive rules for changes in PLD condensate stability.

Main Methods:

Utilized a residue-resolution coarse-grained model (Mpipi) for simulations.
Analyzed 140 PLD mutants from six key proteins (hnRNPA1, TDP43, FUS, EWSR1, RBM14, TIA1).

Main Results:

Discovered scaling laws that correlate mutation number and type with critical solution temperature changes in PLDs.
Observed consistency between scaling laws and mutation physicochemical properties across diverse proteins.
Demonstrated that these rules apply broadly across the tested protein family.

Conclusions:

Scaling laws offer a predictive tool for assessing the impact of mutations on PLD condensate stability.
Quantitative analysis reveals how molecular changes influence the emergent behavior of PLD solutions.
Understanding these relationships is crucial for deciphering disease mechanisms linked to protein misregulation.