Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1

Hamed Kooshapur; Nila Roy Choudhury; Bernd Simon; Max Mühlbauer; Alexander Jussupow; Noemi Fernandez; Alisha N. Jones; Andre Dallmann; Frank Gabel; Carlo Camilloni; Gracjan Michlewski; Javier F. Caceres; Michael Sattler

doi:10.1038/s41467-018-04871-9

Nature Communications (Jun 2018)

Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1

Hamed Kooshapur,
Nila Roy Choudhury,
Bernd Simon,
Max Mühlbauer,
Alexander Jussupow,
Noemi Fernandez,
Alisha N. Jones,
Andre Dallmann,
Frank Gabel,
Carlo Camilloni,
Gracjan Michlewski,
Javier F. Caceres,
Michael Sattler

Affiliations

Hamed Kooshapur: Institute of Structural Biology, Helmholtz Zentrum München
Nila Roy Choudhury: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Bernd Simon: Structural and Computational Biology Unit, European Molecular Biology Laboratory
Max Mühlbauer: Center for Integrated Protein Science Munich at Department Chemie, Technical University of Munich
Alexander Jussupow: Center for Integrated Protein Science Munich at Department Chemie, Technical University of Munich
Noemi Fernandez: MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital
Alisha N. Jones: Institute of Structural Biology, Helmholtz Zentrum München
Andre Dallmann: Institute of Structural Biology, Helmholtz Zentrum München
Frank Gabel: Institut Laue-Langevin
Carlo Camilloni: Center for Integrated Protein Science Munich at Department Chemie, Technical University of Munich
Gracjan Michlewski: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Javier F. Caceres: MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital
Michael Sattler: Institute of Structural Biology, Helmholtz Zentrum München

DOI: https://doi.org/10.1038/s41467-018-04871-9
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 17

Abstract

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hnRNP A1 is an auxiliary factor that promotes the Microprocessor-mediated processing of pri-mir-18a, of the oncomiR-1 cluster. Here the authors employ an integrative structural biology approach and provide insights into the molecular mechanism of how hnRNP A1 facilitates pri-mir-18a biogenesis.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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