The cryo-EM structure of a ribosome–Ski2-Ski3-Ski8 helicase complex
| Autor: | Christian Schmidt, Markus Pech, Alain Jacquier, Katharina Braunger, Quentin Defenouillère, Micheline Fromont-Racine, Vivekanandan Shanmuganathan, André Heuer, Roland Beckmann, Abdelkader Namane, Elena Conti, Thomas Becker, Otto Berninghausen, Eva Kowalinski |
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| Přispěvatelé: | Center for Integrated Protein Science (CIPSM), Technische Universität Munchen - Université Technique de Munich [Munich, Allemagne] (TUM)-Ludwig-Maximilians-Universität München (LMU)-Helmholtz Zentrum München = German Research Center for Environmental Health, Max-Planck-Institut für Biochemie = Max Planck Institute of Biochemistry (MPIB), Max-Planck-Gesellschaft, Génétique des Interactions macromoléculaires / Genetics of Macromolecular Interactions, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), ED 515 - Complexité du vivant, Université Pierre et Marie Curie - Paris 6 (UPMC), We thank the Leibnitz-Rechenzentrum Munich (LRZ) for providing computational services and support. This work was supported by the German Research Council (SFB646 to R.B, T.B., and E.C., GRK1721 to R.B. and E.C., FOR1805 to R.B, and SFB1035 to E.C), by the Max Planck Gesellschaft (E.C.), and by the Agence Nationale de la Recherche (2011-BSV6-011-02 and ANR-14-CE-10-0014-01 to Q.D., A.J., and M.F.-R.). R.B. and E.C. acknowledge support by the Center for Integrated Protein Science Munich (CiPS-M), the Graduate School of Quantitative Biosciences Munich (QBM), and the European Research Council (Advanced Grants CRYOTRANSLATION and DEAD2THEEND). We also acknowledge the support of Ph.D. and postdoctoral fellowships from Boehringer Ingelheim Fonds (to C.S. and K.B.), from QBM (to V.S.), from the Ministère de l’Enseignement Supérieur et de la Recherche and from the Fondation ARC pour la Recherche sur le Cancer (to Q.D.), and from EMBO, Marie Curie, and the Daimler und Benz Stiftung (to E.K.)., ANR-11-BSV6-0011,NGD-NSD,Rôle du NSD/NGD: identification des gènes cibles et des facteurs impliqués dans ces mécanismes chez Saccharomyces cerevisiae(2011), ANR-14-CE10-0014,CLEANMD,Mécanismes moléculaires et impact de la voie de dégradation des ARNm nonsense (NMD) sur le transcriptome eucaryote.(2014), Technical University of Munich (TUM)-Ludwig Maximilian University of Munich [Germany] (LMU München)-Helmholtz-Zentrum München (HZM), Max-Planck-Institut für Biochemie (MPIB), Génétique des Interactions macromoléculaires, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Technische Universität Munchen - Université Technique de Munich [Munich, Allemagne] (TUM)-Helmholtz-Zentrum München (HZM)-Ludwig Maximilian University of Munich [Germany] (LMU München) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Protein Conformation RNA Stability [SDV]Life Sciences [q-bio] MESH: DNA Helicases Saccharomyces cerevisiae Ribosome 03 medical and health sciences MESH: Saccharomyces cerevisiae Proteins MESH: Protein Conformation RNA Messenger Ski complex MESH: RNA Messenger Messenger RNA Multidisciplinary biology Exosome Multienzyme Ribonuclease Complex MESH: RNA Fungal Cryoelectron Microscopy DNA Helicases Helicase Nuclear Proteins RNA Fungal MESH: RNA Stability Ribosomal RNA Ribosome Subunits Large Eukaryotic Molecular biology RNA Helicase A MESH: Saccharomyces cerevisiae Cell biology 030104 developmental biology MESH: Exosome Multienzyme Ribonuclease Complex MESH: Ribosome Subunits Large Eukaryotic RNA Ribosomal TRAMP complex biology.protein MESH: RNA Ribosomal MESH: Cryoelectron Microscopy Eukaryotic Ribosome MESH: Nuclear Proteins |
| Zdroj: | Science Science, 2016, 354 (6318), pp.1431-1433. ⟨10.1126/science.aaf7520⟩ Europe PubMed Central Science, American Association for the Advancement of Science, 2016, 354 (6318), pp.1431-1433. ⟨10.1126/science.aaf7520⟩ |
| ISSN: | 0036-8075 1095-9203 |
| DOI: | 10.1126/science.aaf7520⟩ |
| Popis: | Getting rid of faulty mRNA The cell monitors the health of its mRNAs, destroying those that are faulty or damaged. Destruction by the exosome complex prevents them from being used to synthesize deranged and potentially dangerous proteins. Schmidt et al. determined the structure of the Ski helicase complex, which guides RNAs to the exosome complex destruction machinery in association with a mRNAbound ribosome. The end of the mRNA is threaded from the ribosome into the heart of the helicase, whence the message would be channeled into the maw of the exosome complex. Science , this issue p. 1431 |
| Databáze: | OpenAIRE |
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