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

Anne-Emmanuelle Foucher, Leila Touat-Todeschini, Ariadna B. Juarez-Martinez, Auriane Rakitch, Hamida Laroussi, Claire Karczewski, Samira Acajjaoui, Montserrat Soler-López, Stephen Cusack, Cameron D. Mackereth (), André Verdel () and Jan Kadlec ()
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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

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-32542-3

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