Publications
2017
Edelmann F T, 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 Journal Article
In: Nat Struct Mol Biol, vol. 24, no. 2, pp. 152-161, 2017, ISBN: 28092367.
Abstract | Links | BibTeX | Tags: Cell polarity RNA transport X-ray crystallography, MARQUET, MARQUET PAILLART Cell polarity RNA transport X-ray crystallography, PAILLART, Unité ARN
@article{,
title = {Molecular architecture and dynamics of ASH1-mRNA recognition by its mRNA-transport complex},
author = {F T Edelmann and A Schlundt and R G Heym and A Jenner and A Niedner-Boblenz and M I Syed and J C Paillart and R Stehle and R Janowski and M Sattler and R P Jansen and D Niessing},
url = {https://www.ncbi.nlm.nih.gov/pubmed/28092367?dopt=Abstract},
doi = {10.1038/nsmb.3351},
isbn = {28092367},
year = {2017},
date = {2017-01-01},
journal = {Nat Struct Mol Biol},
volume = {24},
number = {2},
pages = {152-161},
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.},
keywords = {Cell polarity RNA transport X-ray crystallography, MARQUET, MARQUET PAILLART Cell polarity RNA transport X-ray crystallography, PAILLART, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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.