Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex
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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.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Weick, E.-M., Puno, M. R., Januszyk, K., Zinder, J. C., DiMattia, M. A., & Lima, C. D. (2018) · Cell · doi:10.1016/j.cell.2018.05.041 · Cited by 153 · see citing works
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- Authors
- Foucher, A.-E., Touat-Todeschini, L., Juarez-Martinez, A. B., Rakitch, A., Laroussi, H., Karczewski, C., Acajjaoui, S., Soler-López, M., Cusack, S., Mackereth, C. D., Verdel, A., & Kadlec, J.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- European Synchrotron Radiation Facility (FR)
- European Molecular Biology Laboratory (FR)
- Corresponding author
- Mackereth, Cameron D.
- Verdel, André
- Kadlec, Jan
- ORCID
- Venue
- Nature Communications
- Published
- 2022-08-24
- Volume
- 13
- Issue
- 1
- Pages
- 4969-4969
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9402713
- OpenAlex
- W4293103025
- Cited by
- 26
- References
- 2
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 11 · 2023: 7 · 2022: 1
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- HAL (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- European Molecular Biology Laboratory (UAR 3518 CNRS-CEA-UGA-EMBL)
- European Commission (ANR-17-EURE-0003, 2007–2013, UAR 3518 CNRS-CEA-UGA-EMBL, FP7 2007-2013, ANR-13, 609102, FP7/2007)
- Agence Nationale de la Recherche (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, ANR-17-EURE-, ANR-13-BSV2-0012, ANR-21-CE11-0021, ANR-17, ANR-10, ANR-10-LABX, ANR-10-LABX-49-01, ANR-10-INBS-0005, ANR-10-LABX-0049)
- European Synchrotron Radiation Facility
- Centre National de la Recherche Scientifique (Fr3050, IR-RMN-THC Fr3050, ANR-10-LABX-49-01, ANR‐17‐EURE‐0003, UAR 3518 CNRS-CEA-UGA-EMBL)
- Campus France (PCOFUND‐GA‐2013‐609102, FP7/2007-2013)
- French Infrastructure for Integrated Structural Biology (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, ANR-10-INBS-0005, ANR-10-INBS-000502, ANR-10-INBS, ANR-10-LABX-49-01)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Keywords
- Red1, ARS2, Adobe Flash, helix-turn-helix domain, protein-protein interaction, coiled-coil dimerization, exosomes, RNA degradation, Schizosaccharomyces pombe, human homolog
- MeSH terms
- Carrier Proteins, Humans, Meiosis, RNA, RNA, Messenger, Schizosaccharomyces, RNA Stability, Schizosaccharomyces pombe Proteins
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