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5. In Vitro Reconstitution of Eukaryotic Translation Reveals Cooperativity between Release Factors eRF1 and eRF3

Author

Alkalaeva, Elena Z., Pisarev, Andrey V., Frolova, Lyudmila Y., Kisselev, Lev L., and Pestova, Tatyana V.

Subjects
Polypeptides -- Analysis, Hydrolysis -- Analysis, RNA -- Analysis, Guanosine -- Analysis, Biological sciences
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2006.04.035 Byline: Elena Z. Alkalaeva (1)(2), Andrey V. Pisarev (1), Lyudmila Y. Frolova (2), Lev L. Kisselev (2), Tatyana V. Pestova (1)(3) Abstract: Eukaryotic translation termination is triggered by peptide release factors eRF1 and eRF3. Whereas eRF1 recognizes all three termination codons and induces hydrolysis of peptidyl tRNA, eRF3's function remains obscure. Here, we reconstituted all steps of eukaryotic translation in vitro using purified ribosomal subunits; initiation, elongation, and termination factors; and aminoacyl tRNAs. This allowed us to investigate termination using pretermination complexes assembled on mRNA encoding a tetrapeptide and to propose a model for translation termination that accounts for the cooperative action of eRF1 and eRF3 in ensuring fast release of nascent polypeptide. In this model, binding of eRF1, eRF3, and GTP to pretermination complexes first induces a structural rearrangement that is manifested as a 2 nucleotide forward shift of the toeprint attributed to pretermination complexes that leads to GTP hydrolysis followed by rapid hydrolysis of peptidyl tRNA. Cooperativity between eRF1 and eRF3 required the eRF3 binding C-terminal domain of eRF1. Author Affiliation: (1) Department of Microbiology and Immunology, SUNY Downstate Medical Center, Brooklyn, NY 11203, USA (2) Engelhardt Institute of Molecular Biology, The Russian Academy of Sciences, 119991 Moscow, Russia (3) A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899 Moscow, Russia Article History: Received 31 January 2006; Revised 21 March 2006; Accepted 18 April 2006 Article Note: (miscellaneous) Published: June 15, 2006

Published
2006

6. Initiation of protein synthesis from the A site of the ribosome

Author

Wilson, Joan E., Pestova, Tatyana V., Hellen, Christopher U. T., and Sarnow, Peter

Subjects
Proteins -- Synthesis, Genetic translation -- Analysis, Ribosomes -- Physiological aspects, Genetic transcription -- Analysis, Biological sciences
Abstract

The assembly of 80S ribosomes in the cricket paralysis virus involves 40S and 60S ribosomal subunits with a CCU and GCU triplets at the P and the A site respectively. Data indicate that although the A site lacks translation initiation factors, initiation of protein synthesis occurs at this site suggesting involvement of unknown factors.

Published
2000

8. Coupled Folding during Translation Initiation

Author

Christopher U.T. Hellen and Tatyana V. Pestova

Subjects
Messenger RNA, EIF4G, Biochemistry, Genetics and Molecular Biology(all), Cell, EIF4E, Biology, Ribosomal RNA, Bioinformatics, General Biochemistry, Genetics and Molecular Biology, Cell biology, Folding (chemistry), chemistry.chemical_compound, medicine.anatomical_structure, Eukaryotic translation, chemistry, Eukaryotic initiation factor, medicine
Abstract

The structure of the eukaryotic initiation factor eIF4E bound to a cognate domain of eIF4G and m 7 GDP in this issue of Cell shows that these factors undergo coupled folding to form a stable complex with high cap binding activity that promotes efficient ribosomal attachment to mRNA during translation initiation.

Published
2003
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9. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3

Author

Lyudmila Frolova, Lev L. Kisselev, Tatyana V. Pestova, Elena Alkalaeva, and Andrey V. Pisarev

Subjects
GTP', Cooperativity, Biology, RNA, Transfer, Amino Acyl, Models, Biological, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Eukaryotic translation, Protein biosynthesis, Animals, Eukaryotic release factors, 030304 developmental biology, 0303 health sciences, Biochemistry, Genetics and Molecular Biology(all), Hydrolysis, 030302 biochemistry & molecular biology, Peptide Termination Factors, Peptide Chain Termination, Translational, Protein Subunits, Terminator (genetics), Biochemistry, Protein Biosynthesis, Transfer RNA, Biophysics, Codon, Terminator, Guanosine Triphosphate, Rabbits, Ribosomes, Protein Binding
Abstract

SummaryEukaryotic translation termination is triggered by peptide release factors eRF1 and eRF3. Whereas eRF1 recognizes all three termination codons and induces hydrolysis of peptidyl tRNA, eRF3's function remains obscure. Here, we reconstituted all steps of eukaryotic translation in vitro using purified ribosomal subunits; initiation, elongation, and termination factors; and aminoacyl tRNAs. This allowed us to investigate termination using pretermination complexes assembled on mRNA encoding a tetrapeptide and to propose a model for translation termination that accounts for the cooperative action of eRF1 and eRF3 in ensuring fast release of nascent polypeptide. In this model, binding of eRF1, eRF3, and GTP to pretermination complexes first induces a structural rearrangement that is manifested as a 2 nucleotide forward shift of the toeprint attributed to pretermination complexes that leads to GTP hydrolysis followed by rapid hydrolysis of peptidyl tRNA. Cooperativity between eRF1 and eRF3 required the eRF3 binding C-terminal domain of eRF1.

Published
2006

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