A unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5′–3′ mRNA exonuclease in yeast
| Autor: | Olga Kolesnikova, Marc Graille, Claudine Gaudon-Plesse, Valerio Taverniti, Régis Back, Zaineb Fourati, Bertrand Séraphin, Clément Charenton |
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| Přispěvatelé: | Laboratoire de Biochimie de l'Ecole polytechnique (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), Université de Strasbourg (UNISTRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Exonuclease RNA Stability RNA-binding protein [SDV.CAN]Life Sciences [q-bio]/Cancer [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology Protein–protein interaction Fungal Proteins 03 medical and health sciences Protein Domains Yeasts P-bodies Endoribonucleases RNA Messenger mRNA decapping Messenger RNA Multidisciplinary C-terminus fungi RNA RNA-Binding Proteins [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Molecular biology [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] Yeast Cell biology 030104 developmental biology PNAS Plus Exoribonucleases biology.protein Eukaryotic mRNA decay Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2017, 114 (45), pp.E9493-E9501. ⟨10.1073/pnas.1711680114⟩ |
| ISSN: | 0027-8424 1091-6490 |
| Popis: | International audience; The Pat1 protein is a central player of eukaryotic mRNA decay that has also been implicated in translational control. It is commonly considered a central platform responsible for the recruitment of several RNA decay factors. We demonstrate here that a yeast-specific C-terminal region from Pat1 interacts with several short motifs, named helical leucine-rich motifs (HLMs), spread in the long C-terminal region of yeast Dcp2 decapping enzyme. Structures of Pat1-HLM complexes reveal the basis for HLM recognition by Pat1. We also identify a HLM present in yeast Xrn1, the main 5'-3' exonuclease involved in mRNA decay. We show further that the ability of yeast Pat1 to bind HLMs is required for efficient growth and normal mRNA decay. Overall, our analyses indicate that yeast Pat1 uses a single binding surface to successively recruit several mRNA decay factors and show that interaction between those factors is highly polymorphic between species. |
| Databáze: | OpenAIRE |
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