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Nat. Struct. Mol. Biol. 24, 152-161 (2017)
Verlagsversion Forschungsdaten DOI
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
Zeitschrift Nature Structural & Molecular Biology
Quellenangaben Band: 24, Heft: 2, Seiten: 152-161
Verlag Nature Publishing Group
Verlagsort New York, NY
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)