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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
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Stabilization of eukaryotic ribosomal termination complexes by deacylated tRNA
Denis Susorov1, Tatiana Mikhailova2, Alexander Ivanov1
1Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, 119991 Moscow, Russia Faculty of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, 119992 Moscow, Russia.
Nucleic Acids Research
|March 11, 2015
Summary
Deacylated tRNAs in the ribosome
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Ribosome stabilization is crucial for translational control.
- Mechanisms for eukaryotic translation initiation and elongation are well-studied.
- Eukaryotic translation termination complex stabilization remains largely unknown.
Purpose of the Study:
- To elucidate mechanisms of eukaryotic translation termination complex stabilization.
- To investigate the role of deacylated tRNAs in termination complex stability.
Main Methods:
- Site-directed mutagenesis of tRNA(Val).
- Construction of mini-helix structures mimicking tRNA acceptor stems.
- Analysis of termination and posttermination complex stability.
Main Results:
- Deacylated tRNAs in the E site enhance termination complex stability.
- Stabilization involves the stop codon-recognizing part of eRF1 in the A site.
- Stabilization is independent of peptidyl-tRNA hydrolysis.
- The tRNA acceptor stem determines this stabilization property.
Conclusions:
- Deacylated tRNAs fine-tune eukaryotic translation termination.
- The tRNA acceptor stem plays a key role in stabilizing termination complexes.
- This mechanism differs from known ribosome stabilization pathways.
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