Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate.

Autor: Seim I; Curriculum in Bioinformatics and Computational Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.; Department of Applied Physical Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599., Posey AE; Department of Biomedical Engineering, Center for Science & Engineering of Living Systems, Washington University in St. Louis, St. Louis, MO 63130., Snead WT; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599., Stormo BM; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599., Klotsa D; Curriculum in Bioinformatics and Computational Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.; Department of Applied Physical Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599., Pappu RV; Department of Biomedical Engineering, Center for Science & Engineering of Living Systems, Washington University in St. Louis, St. Louis, MO 63130., Gladfelter AS; Curriculum in Bioinformatics and Computational Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.; Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Jazyk: angličtina
Zdroj: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Mar 29; Vol. 119 (13), pp. e2120799119. Date of Electronic Publication: 2022 Mar 25.
DOI: 10.1073/pnas.2120799119
Abstrakt: SignificanceA large subclass of biomolecular condensates are linked to RNA regulation and are known as ribonucleoprotein (RNP) bodies. While extensive work has identified driving forces for biomolecular condensate formation, relatively little is known about forces that oppose assembly. Here, using a fungal RNP protein, Whi3, we show that a portion of its intrinsically disordered, glutamine-rich region modulates phase separation by forming transient alpha helical structures that promote the assembly of dilute phase oligomers. These oligomers detour Whi3 proteins from condensates, thereby impacting the driving forces for phase separation, the protein-to-RNA ratio in condensates, and the material properties of condensates. Our findings show how nanoscale conformational and oligomerization equilibria can influence mesoscale phase equilibria.
Databáze: MEDLINE