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mRNA recognition and packaging by the human transcription–export complex

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  • Belén Pacheco-Fiallos

    (Vienna BioCenter (VBC)
    Doctoral School of the University of Vienna and Medical University of Vienna)

  • Matthias K. Vorländer

    (Vienna BioCenter (VBC))

  • Daria Riabov-Bassat

    (Vienna BioCenter (VBC))

  • Laura Fin

    (Vienna BioCenter (VBC))

  • Francis J. O’Reilly

    (Technische Universität Berlin)

  • Farja I. Ayala

    (Vienna BioCenter (VBC)
    Doctoral School of the University of Vienna and Medical University of Vienna)

  • Ulla Schellhaas

    (Vienna BioCenter (VBC)
    Doctoral School of the University of Vienna and Medical University of Vienna)

  • Juri Rappsilber

    (Technische Universität Berlin
    University of Edinburgh)

  • Clemens Plaschka

    (Vienna BioCenter (VBC))

Abstract

Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription–export complex (TREX) for nuclear export1,2. However, the mechanisms of mRNP recognition and three-dimensional mRNP organization are poorly understood3. Here we report cryo-electron microscopy and tomography structures of reconstituted and endogenous human mRNPs bound to the 2-MDa TREX complex. We show that mRNPs are recognized through multivalent interactions between the TREX subunit ALYREF and mRNP-bound exon junction complexes. Exon junction complexes can multimerize through ALYREF, which suggests a mechanism for mRNP organization. Endogenous mRNPs form compact globules that are coated by multiple TREX complexes. These results reveal how TREX may simultaneously recognize, compact and protect mRNAs to promote their packaging for nuclear export. The organization of mRNP globules provides a framework to understand how mRNP architecture facilitates mRNA biogenesis and export.

Suggested Citation

  • Belén Pacheco-Fiallos & Matthias K. Vorländer & Daria Riabov-Bassat & Laura Fin & Francis J. O’Reilly & Farja I. Ayala & Ulla Schellhaas & Juri Rappsilber & Clemens Plaschka, 2023. "mRNA recognition and packaging by the human transcription–export complex," Nature, Nature, vol. 616(7958), pages 828-835, April.
    • Handle: RePEc:nat:nature:v:616:y:2023:i:7958:d:10.1038_s41586-023-05904-0
    DOI: 10.1038/s41586-023-05904-0
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    Cited by:

    1. Ebru Aydin & Silke Schreiner & Jacqueline Böhme & Birte Keil & Jan Weber & Bojan Žunar & Timo Glatter & Cornelia Kilchert, 2024. "DEAD-box ATPase Dbp2 is the key enzyme in an mRNP assembly checkpoint at the 3’-end of genes and involved in the recycling of cleavage factors," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Olivier Bensaude & Isabelle Barbosa & Lucia Morillo & Rivka Dikstein & Hervé Hir, 2024. "Exon-junction complex association with stalled ribosomes and slow translation-independent disassembly," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Elizabeth A. Werren & Geneva R. LaForce & Anshika Srivastava & Delia R. Perillo & Shaokun Li & Katherine Johnson & Safa Baris & Brandon Berger & Samantha L. Regan & Christian D. Pfennig & Sonja Munnik, 2024. "TREX tetramer disruption alters RNA processing necessary for corticogenesis in THOC6 Intellectual Disability Syndrome," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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