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12. Реформа образования: физико-математические науки

Author

Елисеев Борис Петрович, ФГБОУ ВО «Московский государственный технический университет гражданской авиации», Eliseev Boris Petrovich, FSBEI of HE «Moscow State Technical University of Civil Aviation», Елисеев Борис Петрович, ФГБОУ ВО «Московский государственный технический университет гражданской авиации», Eliseev Boris Petrovich, and FSBEI of HE «Moscow State Technical University of Civil Aviation» more...

Abstract

В статье рассматривается ряд новых проблем, возникающих вследствие происходящей реформы отечественного образования, связанных с необходимостью усиления физико-математической подготовки в средней и высшей школе. more...

Published
2014

16. Backbone H, C and N resonance assignments of the human eukaryotic release factor eRF1.

Author

Polshakov, Vladimir, Eliseev, Boris, Frolova, Ludmila, Chang, Chi-Fon, and Huang, Tai-huang

Abstract

Eukaryotic translation termination is mediated by two interacting release factors, eukaryotic class 1 release factor (eRF1) and eukaryotic class 3 release factor (eRF3), which act cooperatively to ensure efficient stop codon recognition and fast polypeptide release. eRF1 consisting of three well-defined functional domains recognizes all three mRNA stop codons located in the A site of the small ribosomal subunit and triggers hydrolysis of the ester bond of peptidyl-tRNA in the peptidyl transfer center of the large ribosomal subunit. Nevertheless, various aspects of molecular mechanism of translation termination in eukaryotes remain unclear. Elucidation of the structure and dynamics of eRF1 in solution is essential for understanding molecular mechanism of its function in translation termination. To approach this problem, here we report NMR backbone signal assignments of the human eRF1 (437 a.a., 50 kDa). [ABSTRACT FROM AUTHOR] more...

Published
2015
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17. Structure of a human cap-dependent 48S translation pre-initiation complex

Author

Eliseev, Boris, Yeramala, Lahari, Leitner, Alexander, Karuppasamy, Manikandan, Raimondeau, Etienne, Huard, Karine, Alkalaeva, Elena, Aebersold, Ruedi, and Schaffitzel, Christiane

Subjects
3. Good health
Abstract

Eukaryotic translation initiation is tightly regulated, requiring a set of conserved initiation factors (eIFs). Translation of a capped mRNA depends on the trimeric eIF4F complex and eIF4B to load the mRNA onto the 43S pre-initiation complex comprising 40S and initiation factors 1, 1A, 2, 3 and 5 as well as initiator-tRNA. Binding of the mRNA is followed by mRNA scanning in the 48S pre-initiation complex, until a start codon is recognised. Here, we use a reconstituted system to prepare human 48S complexes assembled on capped mRNA in the presence of eIF4B and eIF4F. The highly purified h-48S complexes are used for cross-linking/mass spectrometry, revealing the protein interaction network in this complex. We report the electron cryo-microscopy structure of the h-48S complex at 6.3 Å resolution. While the majority of eIF4B and eIF4F appear to be flexible with respect to the ribosome, additional density is detected at the entrance of the 40S mRNA channel which we attribute to the RNA-recognition motif of eIF4B. The eight core subunits of eIF3 are bound at the 40S solvent-exposed side, as well as the subunits eIF3d, eIF3b and eIF3i. elF2 and initiator-tRNA bound to the start codon are present at the 40S intersubunit side. This cryo-EM structure represents a molecular snap-shot revealing the h-48S complex following start codon recognition., Nucleic Acids Research, 46 (5), ISSN:1362-4962, ISSN:0301-5610 more...