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TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export

Author

Listed:
  • Nicolas Viphakone

    (The University of Sheffield, Firth Court, Western Bank)

  • Guillaume M. Hautbergue

    (The University of Sheffield, Firth Court, Western Bank)

  • Matthew Walsh

    (The University of Sheffield, Firth Court, Western Bank)

  • Chung-Te Chang

    (The University of Sheffield, Firth Court, Western Bank)

  • Arthur Holland

    (The University of Sheffield, Firth Court, Western Bank)

  • Eric G. Folco

    (Harvard Medical School)

  • Robin Reed

    (Harvard Medical School)

  • Stuart A. Wilson

    (The University of Sheffield, Firth Court, Western Bank)

Abstract

The metazoan TREX complex is recruited to mRNA during nuclear RNA processing and functions in exporting mRNA to the cytoplasm. Nxf1 is an mRNA export receptor, which binds processed mRNA and transports it through the nuclear pore complex. At present, the relationship between TREX and Nxf1 is not understood. Here we show that Nxf1 uses an intramolecular interaction to inhibit its own RNA-binding activity. When the TREX subunits Aly and Thoc5 make contact with Nxf1, Nxf1 is driven into an open conformation, exposing its RNA-binding domain, allowing RNA binding. Moreover, the combined knockdown of Aly and Thoc5 markedly reduces the amount of Nxf1 bound to mRNA in vivo and also causes a severe mRNA export block. Together, our data indicate that TREX provides a license for mRNA export by driving Nxf1 into a conformation capable of binding mRNA.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2005
    DOI: 10.1038/ncomms2005
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    1. 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.
    2. Liang Chen & Yucong Wang & Jiamei Lin & Zhenxing Song & Qinwei Wang & Wenfang Zhao & Yan Wang & Xiaoyu Xiu & Yuqi Deng & Xiuzhi Li & Qiqi Li & Xiaolin Wang & Jingxin Li & Xu Liu & Kunpeng Liu & Jincon, 2022. "Exportin 4 depletion leads to nuclear accumulation of a subset of circular RNAs," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    3. Simeon R. Mihaylov & Lydia M. Castelli & Ya-Hui Lin & Aytac Gül & Nikita Soni & Christopher Hastings & Helen R. Flynn & Oana Păun & Mark J. Dickman & Ambrosius P. Snijders & Robert Goldstone & Oliver, 2023. "The master energy homeostasis regulator PGC-1α exhibits an mRNA nuclear export function," Nature Communications, Nature, vol. 14(1), pages 1-22, December.

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