Possible steps of complete disassembly of post-termination complex by yeast eEF3 deduced from inhibition by translocation inhibitors
| Autor: | Nono Takeuchi, Hideko Kaji, Ben Shen, Jun O. Liu, Shinya Kurata, Akira Kaji |
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| Rok vydání: | 2012 |
| Předmět: |
Paromomycin
Saccharomyces cerevisiae Biology Cycloheximide Ribosome Fungal Proteins chemistry.chemical_compound Adenosine Triphosphate RNA Transfer Polysome Genetics RNA Messenger Molecular Biology Piperidones Protein Synthesis Inhibitors Translation (biology) Peptide Chain Termination Translational Peptide Elongation Factors Indenes Peptide Elongation Factor 2 chemistry Biochemistry Puromycin Transfer RNA Lactimidomycin Macrolides Fusidic Acid Ribosomes Peptide Termination Factors |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | Ribosomes, after one round of translation, must be recycled so that the next round of translation can occur. Complete disassembly of post-termination ribosomal complex (PoTC) in yeast for the recycling consists of three reactions: release of tRNA, release of mRNA and splitting of ribosomes, catalyzed by eukaryotic elongation factor 3 (eEF3) and ATP. Here, we show that translocation inhibitors cycloheximide and lactimidomycin inhibited all three reactions. Cycloheximide is a non-competitive inhibitor of both eEF3 and ATP. The inhibition was observed regardless of the way PoTC was prepared with either release factors or puromycin. Paromomycin not only inhibited all three reactions but also re-associated yeast ribosomal subunits. On the other hand, sordarin or fusidic acid, when applied together with eEF2/GTP, specifically inhibited ribosome splitting without blocking of tRNA/mRNA release. From these inhibitor studies, we propose that, in accordance with eEF3’s known function in elongation, the release of tRNA via exit site occurs first, then mRNA is released, followed by the splitting of ribosomes during the disassembly of post-termination complexes catalyzed by eEF3 and ATP. |
| Databáze: | OpenAIRE |
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