Phase separation of Dri1 contributes to heterochromatin formation in Schizosaccharomyces pombe

The RNA binding protein Dri1 facilitates heterochromatin assembly via the RNAi pathway and histone deacetylases (HDAC). Dri1 contains an intrinsically disordered region (IDR) and three zinc fingers at its C-terminus, which are important for its role in heterochromatin silencing. Both IDR and zinc fi...

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Detalles Bibliográficos
Autores principales: Ban, Hyoju, Sun, Wenqi, Chen, Yong, Li, Fei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2022
Materias:
New Finding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9019594/
https://www.ncbi.nlm.nih.gov/pubmed/35622527
http://dx.doi.org/10.17912/micropub.biology.000559
Descripción
Sumario:The RNA binding protein Dri1 facilitates heterochromatin assembly via the RNAi pathway and histone deacetylases (HDAC). Dri1 contains an intrinsically disordered region (IDR) and three zinc fingers at its C-terminus, which are important for its role in heterochromatin silencing. Both IDR and zinc fingers have been implicated in mediating liquid-liquid phase separation (LLPS). In this study, we investigated the phase separation properties of Dri1. We observed that Dri1 undergoes phase separation in vitro . Dri1 also exhibits liquid-like behavior in vivo . Combined with our previous findings, our data support a model in which the phase-separated condensates formed by Dri1 may help recruit RNAi components and HDAC to mediate heterochromatin assembly.

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