Ribosome-bound Pub1 modulates stop codon decoding during translation termination in yeast
Autor: | Michael D. Ter-Avanesyan, Valery N. Urakov, Irina V. Safenkova, Olga V. Mitkevich |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Translation (biology) Cell Biology Saccharomyces cerevisiae Biology Peptide Chain Termination Translational Biochemistry Ribosome Poly(A)-Binding Proteins Stop codon Cell biology 03 medical and health sciences 030104 developmental biology Stress granule Polysome Prokaryotic translation Codon Terminator Ribosome profiling Translation factor Molecular Biology Ribosomes Peptide Termination Factors Sequence Deletion |
Zdroj: | The FEBS journal. 284(12) |
ISSN: | 1742-4658 |
Popis: | In eukaryotes, termination of translation is controlled by polypeptide chain release factors eRF1 and eRF3, of which the former recognizes nonsense codons, while the latter interacts with eRF1 and stimulates polypeptide release from the ribosome in a GTP- dependent manner, and ABCE1, which facilitates ribosome recycling. In this work, we demonstrate that Pub1, a yeast protein known to be involved in stress granule formation, regulation of gene expression, and organization of the tubulin cytoskeleton, also plays a role in translation termination. Pub1 was shown to bind to ribosomes independent of eRF1 and eRF3 and to interact with the N-terminal glutamine-/asparagine-rich prion domain of eRF3 via its short C-terminal glutamine-rich tract. High velocity sedimentation in sucrose gradient demonstrated that Pub1 was preferentially associated with heavy polysomes enriched with terminating ribosomes. Lack of Pub1 decreased efficiency of nonsense readthrough at a majority but not all tetranucleotide stop signals. This distinguishes Pub1 from most other known binding partners of the release factors which were shown to modulate readthrough of all nonsense codons uniformly. The obtained data show that Pub1 can act as an accessory translation factor involved in fine-tuning of translation termination. |
Databáze: | OpenAIRE |
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