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• W2018384209 abstract "The proteins harboring double-stranded RNA binding domains (dsRBDs) play diverse functional roles such as RNA localization, splicing, editing, export, and translation, yet mechanistic basis and functional significance of dsRBDs remain unclear. To unravel this enigma, we investigated transactivation response RNA binding protein (TRBP) consisting of three dsRBDs, which functions in HIV replication, protein kinase R(PKR)-mediated immune response, and RNA silencing. Here we report an ATP-independent diffusion activity of TRBP exclusively on dsRNA in a length-dependent manner. The first two dsRBDs of TRBP are essential for diffusion, whereas the third dsRBD is dispensable. Two homologs of TRBP, PKR activator and R3D1-L, displayed the same diffusion, implying a universality of the diffusion activity among this protein family. Furthermore, a Dicer-TRBP complex on dsRNA exhibited dynamic diffusion, which was correlated with Dicer's catalytic activity. These results implicate the dsRNA-specific diffusion activity of TRBP that contributes to enhancing siRNA and miRNA processing by Dicer." @default.
• W2018384209 created "2016-06-24" @default.
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• W2018384209 date "2012-12-18" @default.
• W2018384209 modified "2023-10-11" @default.
• W2018384209 title "ATP-independent diffusion of double-stranded RNA binding proteins" @default.
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• W2018384209 doi "https://doi.org/10.1073/pnas.1212917110" @default.
• W2018384209 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3538233" @default.
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