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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)
Verlagsversion Forschungsdaten DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Cell polarity; RNA transport; X-ray crystallography; Cis-acting Determinants; Binding Protein; Translational Repression; Localization Elements; Myosin Motor; Yeast Bud; She2p; Reveals; She3p; Reconstitution
ISSN (print) / ISBN 1545-9993
e-ISSN 1545-9985
Quellenangaben Band: 24, Heft: 2, Seiten: 152-161 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort New York, NY
Begutachtungsstatus Peer reviewed