PuSH - Publikationsserver des Helmholtz Zentrums München: Molecular architecture and dynamics of <em>ASH1</em> mRNA recognition by its mRNA-transport complex.

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Edelmann, F. ; Schlundt, A.* ; Heym, R.G. ; Jenner, A.* ; Niedner-Boblenz, A.* ; Syed, M.I.* ; Paillart, J.C.* ; Stehle, R.* ; Janowski, R. ; Sattler, M. ; Jansen, R.P.* ; Niessing, D.

Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.

Nat. Struct. Mol. Biol. 24, 152-161 (2017)

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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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