Prefabrication of a ribosomal protein subcomplex essential for eukaryotic ribosome formation
| Autor: | Ute Fischer, Yiming Chang, Sabina Schütz, Vikram Govind Panse, Cohue Peña |
|---|---|
| Přispěvatelé: | University of Zurich, Panse, Vikram G |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Ribosomal Proteins
0301 basic medicine Saccharomyces cerevisiae Proteins Macromolecular Substances QH301-705.5 Science ATPases S. cerevisiae 610 Medicine & health Saccharomyces cerevisiae Biology Biochemistry General Biochemistry Genetics and Molecular Biology Ribosome assembly 03 medical and health sciences Tsr2 Eukaryotic translation 1300 General Biochemistry Genetics and Molecular Biology Eukaryotic initiation factor 2400 General Immunology and Microbiology Fap7 Eukaryotic Small Ribosomal Subunit Biology (General) 50S Genetics protein complexes General Immunology and Microbiology 10179 Institute of Medical Microbiology General Neuroscience Adenylate Kinase Nuclear Proteins 2800 General Neuroscience General Medicine Nucleoside-Triphosphatase Cell biology eukaryotic ribosomal proteins Internal ribosome entry site A-site 030104 developmental biology 570 Life sciences biology Medicine Protein Multimerization Eukaryotic Ribosome ribosome assembly Ribosomes Research Article |
| Zdroj: | eLife, Vol 5 (2016) eLife, 5 eLife |
| ISSN: | 2050-084X |
| Popis: | Spatial clustering of ribosomal proteins (r-proteins) through tertiary interactions is a striking structural feature of the eukaryotic ribosome. However, the functional importance of these intricate inter-connections, and how they are established is currently unclear. Here, we reveal that a conserved ATPase, Fap7, organizes interactions between neighboring r-proteins uS11 and eS26 prior to their delivery to the earliest ribosome precursor, the 90S. In vitro, uS11 only when bound to Fap7 becomes competent to recruit eS26 through tertiary contacts found between these r-proteins on the mature ribosome. Subsequently, Fap7 ATPase activity unloads the uS11:eS26 subcomplex onto its rRNA binding site, and therefore ensures stoichiometric integration of these r-proteins into the 90S. Fap7-depletion in vivo renders uS11 susceptible to proteolysis, and precludes eS26 incorporation into the 90S. Thus, prefabrication of a native-like r-protein subcomplex drives efficient and accurate construction of the eukaryotic ribosome. eLife, 5 ISSN:2050-084X |
| Databáze: | OpenAIRE |
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