Pby1 is a direct partner of the Dcp2 decapping enzyme
| Autor: | Loreline Cosson, Bertrand Séraphin, Clément Charenton, Claudine Gaudon-Plesse, Nathalie Ulryck, Régis Back, Marc Graille |
|---|---|
| Přispěvatelé: | Arnoux, Aurélien, BLANC - Mécanisme de clivage de la coiffe des ARNm eucaryotes - - Decapping2011 - ANR-11-BSV8-0009 - BLANC - VALID, Initiative d'excellence - Par-delà les frontières, l'Université de Strasbourg - - UNISTRA2010 - ANR-10-IDEX-0002 - IDEX - VALID, Laboratoire de Biologie Structurale de la Cellule (BIOC), École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Ligue Contre le Cancer (Equipe Labellisée 2020), Ecole Polytechnique, Centre National pour la Recherche Scientifique, CERBM-IGBMC, INSERM, ANR-11-BSV8-0009,Decapping,Mécanisme de clivage de la coiffe des ARNm eucaryotes(2011), ANR-10-IDEX-0002,UNISTRA,Par-delà les frontières, l'Université de Strasbourg(2010) |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins AcademicSubjects/SCI00010 Mutant Protein domain Saccharomyces cerevisiae [SDV.BC]Life Sciences [q-bio]/Cellular Biology Plasma protein binding Biology [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Ligases 03 medical and health sciences Adenosine Triphosphate 0302 clinical medicine Protein Domains Structural Biology Catalytic Domain Endopeptidases Endoribonucleases Genetics [SDV.BC] Life Sciences [q-bio]/Cellular Biology 030304 developmental biology Organelles chemistry.chemical_classification 0303 health sciences Messenger RNA [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Translation (biology) Cell biology DNA-Binding Proteins Decapping complex Enzyme chemistry RNA splicing Holoenzymes 030217 neurology & neurosurgery Protein Binding Transcription Factors |
| Zdroj: | 'Nucleic Acids Research ', vol: 48, pages: 6353-6366 (2020) Nucleic Acids Research Nucleic Acids Research, 2020, 48 (11), ⟨10.1093/nar/gkaa337⟩ Nucleic Acids Research, Oxford University Press, 2020, 48 (11), ⟨10.1093/nar/gkaa337⟩ |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | Most eukaryotic mRNAs harbor a characteristic 5′ m7GpppN cap that promotes pre-mRNA splicing, mRNA nucleocytoplasmic transport and translation while also protecting mRNAs from exonucleolytic attacks. mRNA caps are eliminated by Dcp2 during mRNA decay, allowing 5′-3′ exonucleases to degrade mRNA bodies. However, the Dcp2 decapping enzyme is poorly active on its own and requires binding to stable or transient protein partners to sever the cap of target mRNAs. Here, we analyse the role of one of these partners, the yeast Pby1 factor, which is known to co-localize into P-bodies together with decapping factors. We report that Pby1 uses its C-terminal domain to directly bind to the decapping enzyme. We solved the structure of this Pby1 domain alone and bound to the Dcp1–Dcp2–Edc3 decapping complex. Structure-based mutant analyses reveal that Pby1 binding to the decapping enzyme is required for its recruitment into P-bodies. Moreover, Pby1 binding to the decapping enzyme stimulates growth in conditions in which decapping activation is compromised. Our results point towards a direct connection of Pby1 with decapping and P-body formation, both stemming from its interaction with the Dcp1–Dcp2 holoenzyme. |
| Databáze: | OpenAIRE |
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