Key result
The presence of folded RRM domains and a solubility-tag modifies the phase behavior of hnRNPA1 and reverses the salt dependence of the driving force for phase separation relative to the LCD alone.
Why the study?
Intrinsically disordered low-complexity domains often mediate phase separation, but how their phase behavior is modulated by folded domains is incompletely understood.
Population
RNA-binding protein hnRNPA1
Comparison
Folded RRM domains and folded solubility-tag vs low-complexity domain alone
Design
In vitro small-angle X-ray scattering experiments and coarse-grained MD simulations
Authors
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Modifies in vitro models of hnRNPA1 phase separation; leaves open relevance to cellular condensates or disease.
This basic science study demonstrates that folded domains can significantly modify the phase separation behavior of intrinsically disordered domains, altering their dependence on solution conditions like salt concentration.
Martin et al. (2021) studied this question. Folded RRM domains and solubility-tag vs. Low-complexity domain (LCD) alone was evaluated on Phase separation behavior and salt dependence. The presence of folded RRM domains and a solubility-tag modifies the phase behavior of hnRNPA1 and reverses the salt dependence of the driving force for phase separation relative to the LCD alone.
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