Tho2 is critical for the recruitment of Rrp6 to chromatin in response to perturbed mRNP biogenesis.
Autor: | Beauvais V; Centre de Biophysique Moléculaire, UPR 4301 du CNRS, 45071 Orléans, France., Moreau K; Centre de Biophysique Moléculaire, UPR 4301 du CNRS, 45071 Orléans, France., Žunar B; Laboratory of Biochemistry, Department of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, Zagreb, Croatia., Hervouet-Coste N; Centre de Biophysique Moléculaire, UPR 4301 du CNRS, 45071 Orléans, France., Novačić A; Laboratory of Biochemistry, Department of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, Zagreb, Croatia., Le Dantec A; Centre de Biophysique Moléculaire, UPR 4301 du CNRS, 45071 Orléans, France., Primig M; Univ Rennes, Inserm, EHESP, Irset (Institut de recherche en santé, environnement et travail)-UMR_S 1085, F-2 Rennes, France., Mosrin-Huaman C; Centre de Biophysique Moléculaire, UPR 4301 du CNRS, 45071 Orléans, France., Stuparević I; Laboratory of Biochemistry, Department of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, Zagreb, Croatia istuparevic@pbf.hr., Rahmouni AR; Centre de Biophysique Moléculaire, UPR 4301 du CNRS, 45071 Orléans, France. |
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Jazyk: | angličtina |
Zdroj: | RNA (New York, N.Y.) [RNA] 2023 Dec 18; Vol. 30 (1), pp. 89-98. Date of Electronic Publication: 2023 Dec 18. |
DOI: | 10.1261/rna.079707.123 |
Abstrakt: | The eukaryotic THO complex coordinates the assembly of so-called messenger RNA-ribonucleoprotein particles (mRNPs), a process that involves cotranscriptional coating of nascent mRNAs with proteins. Once formed, mRNPs undergo a quality control step that marks them either for active transport to the cytoplasm, or Rrp6/RNA exosome-mediated degradation in the nucleus. However, the mechanism behind the quality control of nascent mRNPs is still unclear. We investigated the cotranscriptional quality control of mRNPs in budding yeast by expressing the bacterial Rho helicase, which globally perturbs yeast mRNP formation. We examined the genome-wide binding profiles of the THO complex subunits Tho2, Thp2, Hpr1, and Mft1 upon perturbation of the mRNP biogenesis, and found that Tho2 plays two roles. In addition to its function as a subunit of the THO complex, upon perturbation of mRNP biogenesis Tho2 targets Rrp6 to chromatin via its carboxy-terminal domain. Interestingly, other THO subunits are not enriched on chromatin upon perturbation of mRNP biogenesis and are not necessary for localizing Rrp6 at its target loci. Our study highlights the potential role of Tho2 in cotranscriptional mRNP quality control, which is independent of other THO subunits. Considering that both the THO complex and the RNA exosome are evolutionarily highly conserved, our findings are likely relevant for mRNP surveillance in mammals. (© 2024 Beauvais et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society.) |
Databáze: | MEDLINE |
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