A RanGTP-independent mechanism allows ribosomal protein nuclear import for ribosome assembly
| Autor: | Vikram Govind Panse, Olga T. Schubert, Gabriel Schlenstedt, Michaela Gerber, Cohue Peña, Ute Fischer, Stefanie Caesar, Martin Altvater, Sabina Schütz, Purnima Nerurkar, Yiming Chang |
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| Rok vydání: | 2014 |
| Předmět: |
S. cerevisiae
Ribosome biogenesis Biochemistry Ribosome assembly Diamond-Blackfan anemia Ribosome profiling eS26 Biology (General) rRNA processing 0303 health sciences Protein Stability General Neuroscience GTPase-Activating Proteins 030302 biochemistry & molecular biology Diamond-Blackfan anemia (DBA) General Medicine beta Karyopherins Recombinant Proteins Cell biology Medicine Eukaryotic Ribosome Research Article Protein Binding Ribosomal Proteins Saccharomyces cerevisiae Proteins QH301-705.5 Science Molecular Sequence Data Active Transport Cell Nucleus ribosome biogenesis Saccharomyces cerevisiae Importin Karyopherins Biology General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Tsr2 Ribosomal protein Escherichia coli RNA Ribosomal 18S Amino Acid Sequence 030304 developmental biology Cell Nucleus General Immunology and Microbiology E. coli Cell Biology nuclear import Internal ribosome entry site Proteolysis Nuclear transport Carrier Proteins Ribosomes |
| Zdroj: | eLife eLife, Vol 3 (2014) eLIFE eLife, 3 |
| ISSN: | 2050-084X |
| DOI: | 10.7554/eLife.03473 |
| Popis: | Within a single generation time a growing yeast cell imports ∼14 million ribosomal proteins (r-proteins) into the nucleus for ribosome production. After import, it is unclear how these intrinsically unstable and aggregation-prone proteins are targeted to the ribosome assembly site in the nucleolus. Here, we report the discovery of a conserved nuclear carrier Tsr2 that coordinates transfer of the r-protein eS26 to the earliest assembling pre-ribosome, the 90S. In vitro studies revealed that Tsr2 efficiently dissociates importin:eS26 complexes via an atypical RanGTP-independent mechanism that terminates the import process. Subsequently, Tsr2 binds the released eS26, shields it from proteolysis, and ensures its safe delivery to the 90S pre-ribosome. We anticipate similar carriers—termed here escortins—to securely connect the nuclear import machinery with pathways that deposit r-proteins onto developing pre-ribosomal particles. eLife, 3 ISSN:2050-084X |
| Databáze: | OpenAIRE |
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