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Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex

Author

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  • Anne-Emmanuelle Foucher

    (Univ. Grenoble Alpes, CNRS, CEA, IBS)

  • Leila Touat-Todeschini

    (UMR Inserm U1209/CNRS 5309/University Grenoble Alpes)

  • Ariadna B. Juarez-Martinez

    (Univ. Grenoble Alpes, CNRS, CEA, IBS)

  • Auriane Rakitch

    (UMR Inserm U1209/CNRS 5309/University Grenoble Alpes)

  • Hamida Laroussi

    (Univ. Grenoble Alpes, CNRS, CEA, IBS)

  • Claire Karczewski

    (UMR Inserm U1209/CNRS 5309/University Grenoble Alpes)

  • Samira Acajjaoui

    (Structural Biology Group, European Synchrotron Radiation Facility (ESRF))

  • Montserrat Soler-López

    (Structural Biology Group, European Synchrotron Radiation Facility (ESRF))

  • Stephen Cusack

    (European Molecular Biology Laboratory)

  • Cameron D. Mackereth

    (Univ. Bordeaux, Inserm U1212, CNRS UMR 5320, ARNA Laboratory, Institut Européen de Chimie et Biologie)

  • André Verdel

    (UMR Inserm U1209/CNRS 5309/University Grenoble Alpes)

  • Jan Kadlec

    (Univ. Grenoble Alpes, CNRS, CEA, IBS)

Abstract

To eliminate specific or aberrant transcripts, eukaryotes use nuclear RNA-targeting complexes that deliver them to the exosome for degradation. S. pombe MTREC, and its human counterpart PAXT, are key players in this mechanism but inner workings of these complexes are not understood in sufficient detail. Here, we present an NMR structure of an MTREC scaffold protein Red1 helix-turn-helix domain bound to the Iss10 N-terminus and show this interaction is required for proper cellular growth and meiotic mRNA degradation. We also report a crystal structure of a Red1-Ars2 complex explaining mutually exclusive interactions of hARS2 with various ED/EGEI/L motif-possessing RNA regulators, including hZFC3H1 of PAXT, hFLASH or hNCBP3. Finally, we show that both Red1 and hZFC3H1 homo-dimerize via their coiled-coil regions indicating that MTREC and PAXT likely function as dimers. Our results, combining structures of three Red1 interfaces with in vivo studies, provide mechanistic insights into conserved features of MTREC/PAXT architecture.

Suggested Citation

  • Anne-Emmanuelle Foucher & Leila Touat-Todeschini & Ariadna B. Juarez-Martinez & Auriane Rakitch & Hamida Laroussi & Claire Karczewski & Samira Acajjaoui & Montserrat Soler-López & Stephen Cusack & Cam, 2022. "Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32542-3
    DOI: 10.1038/s41467-022-32542-3
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    1. Komal Soni & Anusree Sivadas & Attila Horvath & Nikolay Dobrev & Rippei Hayashi & Leo Kiss & Bernd Simon & Klemens Wild & Irmgard Sinning & Tamás Fischer, 2023. "Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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