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EMBO Rep. 2019 Jan;20(1). pii: e46588. doi: 10.15252/embr.201846588. Epub 2018 Dec 14.

The key protein of endosomal mRNP transport Rrm4 binds translational landmark sites of cargo mRNAs.

Author information

1
Institute for Microbiology, Cluster of Excellence on Plant Sciences, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
2
Buchmann Institute for Molecular Life Sciences (BMLS), Goethe University Frankfurt, Frankfurt am Main, Germany.
3
The Francis Crick Institute, London, UK.
4
Department of Molecular Neuroscience, UCL Institute of Neurology, London, UK.
5
Institute of Molecular Biology gGmbH, Mainz, Germany.
6
Medical Clinic II (Molecular Pneumology), Excellence Cluster Cardio-Pulmonary System, Justus Liebig University of Gießen, Gießen, Germany.
7
Institute for Microbiology, Cluster of Excellence on Plant Sciences, Heinrich Heine University Düsseldorf, Düsseldorf, Germany feldbrue@hhu.de kathi.zarnack@bmls.de.
8
Buchmann Institute for Molecular Life Sciences (BMLS), Goethe University Frankfurt, Frankfurt am Main, Germany feldbrue@hhu.de kathi.zarnack@bmls.de.

Abstract

RNA-binding proteins (RBPs) determine spatiotemporal gene expression by mediating active transport and local translation of cargo mRNAs. Here, we cast a transcriptome-wide view on the transported mRNAs and cognate RBP binding sites during endosomal messenger ribonucleoprotein (mRNP) transport in Ustilago maydis Using individual-nucleotide resolution UV crosslinking and immunoprecipitation (iCLIP), we compare the key transport RBP Rrm4 and the newly identified endosomal mRNP component Grp1 that is crucial to coordinate hyphal growth. Both RBPs bind predominantly in the 3' untranslated region of thousands of shared cargo mRNAs, often in close proximity. Intriguingly, Rrm4 precisely binds at stop codons, which constitute landmark sites of translation, suggesting an intimate connection of mRNA transport and translation. Towards uncovering the code of recognition, we identify UAUG as specific binding motif of Rrm4 that is bound by its third RRM domain. Altogether, we provide first insights into the positional organisation of co-localising RBPs on individual cargo mRNAs.

KEYWORDS:

iCLIP ; RNA transport; endosome; fungus

PMID:
30552148
PMCID:
PMC6322384
[Available on 2020-01-01]
DOI:
10.15252/embr.201846588

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