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Nat Struct Mol Biol. 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.

Author information

1
Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
2
Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Department Chemie, Technische Universität München, Garching, Germany.
3
Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
4
Biomedical Center of the Ludwig-Maximilians-Universität München, Department of Cell Biology, Planegg-Martinsried, Germany.
5
Architecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.

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.

PMID:
28092367
DOI:
10.1038/nsmb.3351
[Indexed for MEDLINE]

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