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The most cited biological Institute in Russia *
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it belongs to: Department of Chemistry and Biochemistry of Nucleoproteins
master: Grand PhD (Chemistry), professor, Ivan N. Shatsky

Laboratory of Protein Synthesis Regulation (head Ivan N. Shatsky) is concerned with mechanisms of translation in eukaryotes and translational control. The officially registered  subject of investigations : “Studies of structure of mRNAs and their complexes with ribosomes”. Until 1989,  the group was concerned with the structure of bacterial ribosomes. From 1989, it started working in the area of translation initiation and its regulation in eukaryotes. Among its principal achievements are:

  1. I. Shatsky and his colleagues established in 1983 for the first time that the mRNA forms a U-turn or loop as it passes through the small ribosomal subunit.
  2. He and his colleagues proposed in 1996 a new in vitro approach to dissect translation initiation mechanisms in mammalian cells. It is based on the reconstitution of translation initiation complexes from individual purified components combined with toeprinting or RelE printing. Using this method, mechanisms of internal initiation of translation used by some picornavirus genomic RNAs has been dissected in 1996-2004.
  3. Pestova et al. (1998) and Terenin et al. (2008) discovered that the hepatitis C virus RNA can use a simplified bacteria-like mode of translation initiation and can do without ubiquitous factor eIF2. 
  4. Dmitriev et al. (2010) discovered a new eukaryotic translation factor, termed by the authors eIF2D, which, unlike all known translation factors is GTP-independent. Its function is still mysterious but preliminary data suggest that it is implicated in meiosis.
  5. Andreev et al. (2011) made a surprising observation that the RNA of poliovirus and presumably of all other members of entero- and rhinoviruses form a highly specific complex with glycyl-tRNA synthetase. This interaction is necessary for activation of translation initiation on these viral RNAs.
  6. In 2010, after extensive study of several mammalian mRNAs having long and highly structured 5’-untranslated regions, a novel model of cap-independent translation initiation mechanism was proposed that does not involve internal ribosome entry. RNA structures that provide the cap-independence but does not provide 5’-end independence (contrary to “true” IRESes) have been named CITEs (cap-independent translational enhancers).

Finally, the lab has recently initiated search of specific mRNAs that use non-canonical translation mechanisms under stress conditions using deep sequencing including the ribosome profiling suggested by Ingolia and co-workers (Science 2009).

The laboratory collaborates with colleagues from USA, Germany, Denmark, Spain, UK, Ireland, as well with a number of Russian laboratories from Moscow, Puschino and Novosibirsk. It has especially close collaborations with laboratories of academicians A.S. Spirin and L.P. Ovchinnikov (Institute of Protein Research of RAS, Puschino, Moscow Region), the lab of Dr. G.G. Karpova (Institute of Fundamental Medicine, Novosibirsk) and Dr. M. Niepmann from Institute of Biochemistry, Giessen University, Germany.

Research Support

  • 2011-2013 – Russian Foundation for Basic Research (RFBR), grant 11-04-01010-a « Mechanisms of translation initiation of mammalian mRNAs with highly structured 5’ untranslated regions», head – Shatsky I.N.
  • 2011-2013 – Russian Foundation for Basic Research (RFBR), grant 11-04-91335-NNIO_a « Proteomic studies on the IRES element of poliovirus RNA», head – Shatsky I.N.
  • 2010-2012 – Russian Foundation for Basic Research (RFBR), grant 10-04-01563-a «Start codon selection during translation initiation in eukaryotes: new details of the classical mechanism, and alternative pathways», head – Dmitriev S.E.
  • 2011-2012 – Grant of the President of Russian Federation (MK-5309.2011.4 «Translation initiation in eukaryotes: new proteins and mechanisms», head – Dmitriev S.E.
  • 2010-2012 – Russian Foundation for Basic Research (RFBR), grant 10-04-01572-a «Role of communication of mRNA’s 5’- and 3’-untranslatied regions in m7G-cap dependence of their translation», head – Terenin I.M.
Last Updated on Friday, 11 May 2012 14:14
Recent papers
  1. Yordanova M.M., Wu C., Andreev D.E., Sachs M.S., Atkins J.F. (2015) A Nascent Peptide Signal Responsive to Endogenous Levels of Polyamines Acts to Stimulate Regulatory Frameshifting on Antizyme mRNA. J. Biol. Chem., 290 (29): 17863-17878. >>

  2. Andreev D.E., O'Connor P.B.F, Zhdanov A.V., Dmitriev R.I., Shatsky I.N., Papkovsky D.B., Baranov P.V. (2015) Oxygen and glucose deprivation induces widespread alterations in mRNA translation within 20 minutes. Genome Biol., 16: . >>

  3. Andreev D.E., O'Connor P.B.F, Fahey C., Kenny E.M., Terenin I.M., Dmitriev S.E., Cormican P., Morris D.W., Shatsky I.N., Baranov P.V. (2015) Translation of 5' leaders is pervasive in genes resistant to eIF2 repression. eLife, 4: . >>

  4. Michel A.M., Andreev D.E., Baranov P.V. (2014) Computational approach for calculating the probability of eukaryotic translation initiation from ribo-seq data that takes into account leaky scanning. BMC Bioinformatics, 15: . >>

  5. Shatsky I.N., Dmitriev S.E., Andreev D.E., Terenin I.M. (2014) Transcriptome-wide studies uncover the diversity of modes of mRNA recruitment to eukaryotic ribosomes. Crit. Rev. Biochem. Mol. Biol., 49 (2): 164-177. >>

  6. Terenin I.M., Andreev D.E., Dmitriev S.E., Shatsky I.N. (2013) A novel mechanism of eukaryotic translation initiation that is neither m(7)G-cap-, nor IRES-dependent. Nucleic Acids Res., 41 (3): 1807-1816. >>

  7. Andreev D.E., Dmitriev S.E., Terenin I.M., Shatsky I.N. (2013) Cap-independent translation initiation of Apaf-1 mRNA based on a scanning mechanism is determined by some features of the secondary structure of its 5 ' untranslated region. Biochem.-Moscow, 78 (2): 157-165. >>

  8. Gushchin V.A., Andreev D.E., Taliansky M.E., MacFarlane S.E., Solovyev A.G., Morozov S.Y. (2013) Single amino acid substitution in the tobacco mosaic virus ORF6 protein suppresses formation of complex with eEF1A and cooperative nucleic acids binding in vitro. Dokl. Biochem. Biophys., 448 (1): 1-4. >>

  9. Gushchin V.A., Lukhovitskaya N.I., Andreev D.E., Wright K.M., Taliansky M.E., Solovyev A.G., Morozov S.Y., MacFarlane S.A. (2013) Dynamic localization of two tobamovirus ORF6 proteins involves distinct organellar compartments. J. Gen. Virol., 94: 230-240. >>

  10. Malygin A.A., Shatsky I.N., Karpova G.G. (2013) Proteins of the human 40S ribosomal subunit involved in hepatitis C IRES Binding as revealed from fluorescent labeling. Biochem.-Moscow, 78 (1): 53-59. >>

  11. Shagam L.I., Terenin I.M., Andreev D.E., Dunaevsky J.E., Dmitriev S.E. (2012) In vitro activity of human translation initiation factor eIF4B is not affected by phosphomimetic amino acid substitutions S422D and S422E. Biochimie, 94 (12): 2484-2490. >>

  12. Andreev D.E., Dmitriev S.E., Zinovkin R., Terenin I.M., Shatsky I.N. (2012) The 5 ' untranslated region of Apaf-1 mRNA directs translation under apoptosis conditions via a 5 ' end-dependent scanning mechanism. FEBS Lett., 586 (23): 4139-4143. >>

  13. Andreev D.E., Hirnet J., Terenin I.M., Dmitriev S.E., Niepmann M., Shatsky I.N. (2012) Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation. Nucleic Acids Res., 40 (12): 5602-5614. >>

  14. Dmitriev S.E., Stolboushkina E.A., Terenin I.M., Andreev D.E., Garber M.B., Shatsky I.N. (2011) Archaeal Translation Initiation Factor aIF2 Can Substitute for Eukaryotic eIF2 in Ribosomal Scanning during Mammalian 48S Complex Formation. Journal of Molecular Biology, 413 (1): 106-114.

  15. Vassilenko K.S., Alekhina O.M., Dmitriev S.E., Shatsky I.N., Spirin A.S. (2011) Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation. Nucleic Acids Research, 39 (13): 5555-5567.

  16. Shatsky I.N., Dmitriev S.E., Terenin I.M., Andreev D.E. (2010) Cap- and IRES-Independent Scanning Mechanism of Translation Initiation as an Alternative to the Concept of Cellular IRESs. Molecules and Cells, 30 (4): 285-293.

  17. Dmitriev S.E., Terenin I.M., Andreev D.E., Ivanov P.A., Dunaevsky J.E., Merrick W.C., Shatsky I.N. (2010) GTP-independent tRNA Delivery to the Ribosomal P-site by a Novel Eukaryotic Translation Factor. Journal of Biological Chemistry, 285 (35): 26779-26787.

  18. Bung C., Bochkaeva Z., Terenin I., Zinovkin R., Shatsky I.N., Niepmann M. (2010) Influence of the hepatitis C virus 3 '-untranslated region on IRES-dependent and cap-dependent translation initiation. FEBS Letters, 584 (4): 837-842.

  19. Malygin A.A., Bochkaeva Z.V., Bondarenko E.I., Kossinova O.A., Loktev V.B., Shatsky I.N., Karpova G.G. (2009) Binding of the IRES of hepatitis C virus RNA to the 40S ribosomal subunit: Role of p40. Molecular Biology, 43 (6): 997-1003.

  20. Andreev D.E., Dmitriev S.E., Terenin I.M., Prassolov V.S., Merrick W.C., Shatsky I.N. (2009) Differential contribution of the m(7)G-cap to the 5' end-dependent translation initiation of mammalian mRNAs. Nucleic Acids Research, 37 (18): 6135-6147.

  21. Dmitriev S.E., Andreev D.E., Adyanova Z.V., Terenin I.M., Shatsky I.N. (2009) Efficient cap-dependent translation of mammalian mRNAs with long and highly structured 5'-untranslated regions in vitro and in vivo. Molecular Biology, 43 (1): 108-113.

  22. Babaylova E.S., Graifer D.M., Malygin A.A., Shatsky I.N., Shtahl I., Karpova G. (2009) Molecular environment of the IIId subdomain of the IRES element of hepatitits C virus RNA on the human 40S ribosomal subunit. Russian Journal of Bioorganic Chemistry, 35 (1): 94-102.

  23. Terenin I.M., Dmitriev S.E., Andreev D.E., Shatsky I.N. (2008) Eukaryotic translation initiation machinery can operate in a bacterial-like mode without eIF2. Nature Structural and Molecular Biology, 15 (8): 836-841.

  24. Andreev D.E., Fernandez-miragall O., Ramajo J., Dmitriev S.E., Terenin I.M., Martinez-salas E., Shatsky I.N. (2007) Differential factor requirement to assemble translation initiation complexes at the alternative start codons of foot- and-mouth disease virus RNA. RNA-Publ. RNA Soc., 13 (8): 1366-1374.

  25. Dmitriev S.E., Andreev D.E., Terenin I.M., Olovnikov I.A., Prassolov V.S., Merrick W.C., Shatsky I.N. (2007) Efficient translation initiation directed by the 900-nucleotide-long and GC-rich 5 ' untranslated region of the human retrotransposon LINE-1 mRNA is strictly cap dependent rather than internal ribosome entry site mediated. Molecular and Cellular Biology, 27 (13): 4685-4697.

  26. Olovnikov I.A., Adyanova Z.V., Galimov E.R., Andreev D.E., Terenin I.M., Ivanov D.S., Prassolov V.S., Dmitriev S.E. (2007) Key role of the internal 5'-UTR segment in the transcription activity of the human L1 retrotransposon. Molecular Biology, 41 (3): 453-458.

  27. Andreev D.E., Terenin I.M., Dmitriev S.E., Shatsky I.N. (2006) Similar features in mechanisms of translation initiation of mRNAS in eukaryotic and prokaryotic systems. Molecular Biology, 40 (4): 694-702.

  28. Laletina E.S., Graifer D.M., Malygin A.A., Shatsky I.N., Karpova G.G. (2006) Molecular environment of the subdomain IIIe loop of the RNA IRES element of hepatitis C virus on the human 40S ribosomal subunit. Russian Journal of Bioorganic Chemistry, 32 (3): 280-287.

  29. Andreev D.E., Terenin I.M., Dunaevsky Y.E., Dmitriev S.E., Shatsky I.N. (2006) A leaderless mRNA can bind to mammalian 80S ribosomes and direct polypeptide synthesis in the absence of translation initiation factors. Molecular and Cellular Biology, 26 (8): 3164-3169.

  30. Dmitriev S.E., Bykova N.V., Andreev D.E., Terenin I.M. (2006) Adequate system for investigation of the human retrotransposon L1 mRNA translation initiation in vitro. Molecular Biology, 40 (1): 25-30.

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