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. 2017 Feb;24(2):152-161.
doi: 10.1038/nsmb.3351. Epub 2017 Jan 16.

Molecular Architecture and Dynamics of ASH1 mRNA Recognition by Its mRNA-transport Complex

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Molecular Architecture and Dynamics of ASH1 mRNA Recognition by Its mRNA-transport Complex

Franziska Theresia Edelmann et al. Nat Struct Mol Biol. .

Abstract

mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex.

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