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- W3004642118 abstract "RNA's structural dynamics are critically important in the processing of microRNAs (miRNAs). We and others have demonstrated that non-A-form structural elements and the conformational flexibility they support are necessary for efficient RNA binding and cleavage by the proteins associated with the two major stages of miRNA processing [Roth, 2013; Quarles, 2013; Quarles, 2015]. However, it is unclear whether the flexibility of primary microRNA (pri-miRNA) is necessary to facilitate complex formation with protein partners. Here, we study the flexibility and bending of a primary microRNA (pri-miR-16) in the presence of a small recombinant construct of the DGCR8 protein that binds double stranded RNA (dsRNA) in vitro. This so-called DGCR8-core contains two dsRNA-binding domains (dsRBD) and a C-terminal tail. We use Small Angle X-ray Scattering (SAXS) to measure the conformations of pri-miR-16 in the presence and absence of the DGCR8-core. SAXS provides global structural insights about freely diffusing macromolecules, including complexes, in solution. With contrast variation, SAXS detects only the nucleic acid (NA) component of a protein-NA complex, by masking out the protein contribution to the scattering profile. Using contrast variation SAXS, we find strong evidence that pri-miR-16 bends in the presence of the DGCR8-core. Complementary studies using single molecule FRET (smFRET) experiments confirm this model." @default.
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- W3004642118 date "2020-02-01" @default.
- W3004642118 modified "2023-09-28" @default.
- W3004642118 title "Evidence that Primary Microrna Bends in the Presence of DGCR8 Seen using Both Saxs and FRET Measurements" @default.
- W3004642118 doi "https://doi.org/10.1016/j.bpj.2019.11.1318" @default.
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