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• W2625486009 abstract "Low-complexity (LC) sequences, typically believed to be incapable of assuming structural order, are abundant constituents of the proteomes of all eukaryotic organisms. These sequences have emerged as critical components for formation of meso-scaled, sub-cellular organelles not invested by surrounding membranes, exemplified by RNA granules. We have observed that LC domains of many RNA binding proteins known to be constituents of RNA granules readily form labile cross-β polymers under physiological conditions. Several lines of experimentation have shown that formation of labile, cross-β polymers assembled from LC domain monomers is important for formation of RNA granules. Among the various experiments we have carried out, hydrogel binding assays have evolved as a versatile technique allowing a reliable means of assessing polymer formation and the binding of heterotypic cellular components integral to the formation of RNA granules. This article presents methods allowing for the production of hydrogel droplets composed of LC domain polymers. We further describe methods allowing straightforward assessment for binding of test LC domains to hydrogel droplets by fluorescence microscopy." @default.
• W2625486009 created "2017-06-23" @default.
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• W2625486009 date "2017-08-01" @default.
• W2625486009 modified "2023-09-24" @default.
• W2625486009 title "Cross-β polymerization and hydrogel formation by low-complexity sequence proteins" @default.
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• W2625486009 doi "https://doi.org/10.1016/j.ymeth.2017.06.011" @default.
• W2625486009 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5583018" @default.
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