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Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes

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  • Ken-ichi Fujita

    (Kyoto University, Kyoto
    Fujita Health University
    National Cancer Center Research Institute)

  • Misa Ito

    (Kyoto University, Kyoto)

  • Midori Irie

    (Kyoto University, Kyoto)

  • Kotaro Harada

    (Kyoto University, Kyoto)

  • Naoko Fujiwara

    (Kyoto University, Kyoto)

  • Yuya Ikeda

    (Kyoto University, Kyoto)

  • Hanae Yoshioka

    (Kyoto University, Kyoto)

  • Tomohiro Yamazaki

    (Kyoto University, Kyoto)

  • Masaki Kojima

    (Tokyo University of Pharmacy and Life Sciences)

  • Bunzo Mikami

    (Kyoto University
    Kyoto University)

  • Akila Mayeda

    (Fujita Health University)

  • Seiji Masuda

    (Kyoto University, Kyoto
    Faculty of Agriculture Kindai University, Nara
    Kindai University, Nara
    Kindai University)

Abstract

mRNA export is an essential pathway for the regulation of gene expression. In humans, closely related RNA helicases, UAP56 and URH49, shape selective mRNA export pathways through the formation of distinct complexes, known as apo-TREX and apo-AREX complexes, and their subsequent remodeling into similar ATP-bound complexes. Therefore, defining the unidentified components of the apo-AREX complex and elucidating the molecular mechanisms underlying the formation of distinct apo-complexes is key to understanding their functional divergence. In this study, we identify additional apo-AREX components physically and functionally associated with URH49. Furthermore, by comparing the structures of UAP56 and URH49 and performing an integrated analysis of their chimeric mutants, we exhibit unique structural features that would contribute to the formation of their respective complexes. This study provides insights into the specific structural and functional diversification of these two helicases that diverged from the common ancestral gene Sub2.

Suggested Citation

  • Ken-ichi Fujita & Misa Ito & Midori Irie & Kotaro Harada & Naoko Fujiwara & Yuya Ikeda & Hanae Yoshioka & Tomohiro Yamazaki & Masaki Kojima & Bunzo Mikami & Akila Mayeda & Seiji Masuda, 2024. "Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-023-44217-8
    DOI: 10.1038/s41467-023-44217-8
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    References listed on IDEAS

    as
    1. Nicolas Viphakone & Guillaume M. Hautbergue & Matthew Walsh & Chung-Te Chang & Arthur Holland & Eric G. Folco & Robin Reed & Stuart A. Wilson, 2012. "TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export," Nature Communications, Nature, vol. 3(1), pages 1-14, January.
    2. Ming-Juan Luo & Zhaolan Zhou & Keith Magni & Claudine Christoforides & Juri Rappsilber & Matthias Mann & Robin Reed, 2001. "Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly," Nature, Nature, vol. 413(6856), pages 644-647, October.
    Full references (including those not matched with items on IDEAS)

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