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    Andrei A Korostelev PhD

    TitleAssistant Professor
    InstitutionUniversity of Massachusetts Medical School
    DepartmentBiochemistry and Molecular Pharmacology
    AddressUniversity of Massachusetts Medical School
    55 Lake Avenue North
    Worcester MA 01655
    Phone508-856-2353
      Other Positions
      InstitutionUMMS - Graduate School of Biomedical Sciences
      DepartmentBiochemistry and Molecular Pharmacology

      InstitutionUMMS - Graduate School of Biomedical Sciences
      DepartmentBioinformatics and Computational Biology

      InstitutionUMMS - Graduate School of Biomedical Sciences
      DepartmentInterdisciplinary Graduate Program

      InstitutionUMMS - Programs, Centers and Institutes
      DepartmentRNA Therapeutics Institute

        Biography 
        awards and honors
        Moscow State University1994 - 1995Soros Academic Fellowship
        Moscow State University1996 - 1997I.V. Berezin Young Scientist Award
        RNA Society2010The RNA Society / Scaringe Young Scientist Award, runner-up
        2011Worcester Science Foundation Award
        2012Session Chair, RiboClub-2012, Sherbrooke, Canada
        Overview 
        Narrative

        Structure and Function of the Ribosome

        Visit Korostelev Lab Web Page

        Dr.  Andrei Korostelev, Ph.D.

        Ribosomes, the ancient and universal cellular machines, are responsible for decoding genetic information and synthesizing proteins in all living organisms. A eubacterial ribosome has a molecular weight of approximately 2.5 MDa and consists of about 55 proteins and 3 large RNA molecules. So far, the ribosome is the largest asymmetric macromolecule amenable to crystallographic analyses.

        The multi-step process of translation is not fully understood: only recently, structural details of some steps of translation started to emerge.

        In our lab, we aim at a full structural description of the highly dynamic process of translation. We use X-ray crystallography to obtain snapshots of different functional states of the ribosome and biochemistry to test the hypotheses concerning the mechanisms and dynamics of the ribosome and translation factors. These studies are designed not only to expand our fundamental knowledge of this molecular machine but also to aid in the development of new drugs that target ribosomes.

        Translation termination on the 70S ribosome

        Translation termination on the 70S ribosome.Release factor RF2 (yellow) is bound to the ribosome in response to a stop codon encoded in a messenger RNA (green) located on the small 30S ribosomal subunit (cyan and blue). RF2 is positioned to catalyze the hydrolysis of a peptidyl-tRNA (green and orange) on the large 50S subunit (grey, purple and magenta). An E-site-bound tRNA is in red.

        This structural model was rendered in Pymol and is based on the X-ray structures of 70S translation termination complexes (Korostelev et al., 2008; Laurberg et al., 2008) and a 70S-tRNA complex (Jenner et al., 2010).



        Rotation Projects

        Rotation projects

        We apply X-ray crystallography and biochemical methods to understand the mechanisms employed by the ribosome. Potential rotation projects are 1) to understand various aspects of translation via mutagenesis/biochemical assays, 2) to crystallize and work on determining the structures of translation factors and functional ribosome complexes, and 3) to improve computational methods used to determine crystal structures of macromolecules.

        Feel free to contact the lab for a more detailed discussion.



        Bibliographic 
        selected publications
        List All   |   Timeline
        1. Brilot AF, Korostelev AA, Ermolenko DN, Grigorieff N. Structure of the ribosome with elongation factor G trapped in the pretranslocation state. Proc Natl Acad Sci U S A. 2013 Dec 24; 110(52):20994-9.
          View in: PubMed
        2. Svidritskiy E, Ling C, Ermolenko DN, Korostelev AA. Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome. Proc Natl Acad Sci U S A. 2013 Jul 23; 110(30):12283-8.
          View in: PubMed
        3. Santos N, Zhu J, Donohue JP, Korostelev AA, Noller HF. Crystal Structure of the 70S Ribosome Bound with the Q253P Mutant Form of Release Factor RF2. Structure. 2013 Jul 2; 21(7):1258-63.
          View in: PubMed
        4. Zhou J, Korostelev A, Lancaster L, Noller HF. Crystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3. Curr Opin Struct Biol. 2012 Dec; 22(6):733-42.
          View in: PubMed
        5. Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Stroud RM, Zhang C, Shokat KM, Walter P. Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. BMC Biol. 2011; 9:48.
          View in: PubMed
        6. Korennykh AV, Korostelev AA, Egea PF, Finer-Moore J, Stroud RM, Zhang C, Shokat KM, Walter P. Structural and functional basis for RNA cleavage by Ire1. BMC Biol. 2011; 9:47.
          View in: PubMed
        7. Korostelev AA. Structural aspects of translation termination on the ribosome. RNA. 2011 Aug; 17(8):1409-21.
          View in: PubMed
        8. Zhu J, Korostelev A, Costantino DA, Donohue JP, Noller HF, Kieft JS. Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome. Proc Natl Acad Sci U S A. 2011 Feb 1; 108(5):1839-44.
          View in: PubMed
        9. Korostelev A, Zhu J, Asahara H, Noller HF. Recognition of the amber UAG stop codon by release factor RF1. EMBO J. 2010 Aug 4; 29(15):2577-85.
          View in: PubMed
        10. Korostelev A, Laurberg M, Noller HF. Multistart simulated annealing refinement of the crystal structure of the 70S ribosome. Proc Natl Acad Sci U S A. 2009 Oct 27; 106(43):18195-200.
          View in: PubMed
        11. Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Zhang C, Shokat KM, Stroud RM, Walter P. The unfolded protein response signals through high-order assembly of Ire1. Nature. 2009 Feb 5; 457(7230):687-93.
          View in: PubMed
        12. Korostelev A, Asahara H, Lancaster L, Laurberg M, Hirschi A, Zhu J, Trakhanov S, Scott WG, Noller HF. Crystal structure of a translation termination complex formed with release factor RF2. Proc Natl Acad Sci U S A. 2008 Dec 16; 105(50):19684-9.
          View in: PubMed
        13. Korostelev A, Ermolenko DN, Noller HF. Structural dynamics of the ribosome. Curr Opin Chem Biol. 2008 Dec; 12(6):674-83.
          View in: PubMed
        14. Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF. Structural basis for translation termination on the 70S ribosome. Nature. 2008 Aug 14; 454(7206):852-7.
          View in: PubMed
        15. Korostelev A, Trakhanov S, Asahara H, Laurberg M, Lancaster L, Noller HF. Interactions and dynamics of the Shine Dalgarno helix in the 70S ribosome. Proc Natl Acad Sci U S A. 2007 Oct 23; 104(43):16840-3.
          View in: PubMed
        16. Korostelev A, Noller HF. The ribosome in focus: new structures bring new insights. Trends Biochem Sci. 2007 Sep; 32(9):434-41.
          View in: PubMed
        17. Korostelev A, Noller HF. Analysis of structural dynamics in the ribosome by TLS crystallographic refinement. J Mol Biol. 2007 Nov 2; 373(4):1058-70.
          View in: PubMed
        18. Korostelev A, Trakhanov S, Laurberg M, Noller HF. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell. 2006 Sep 22; 126(6):1065-77.
          View in: PubMed
        19. Murray S, Nilsson CL, Hare JT, Emmett MR, Korostelev A, Ongley H, Marshall AG, Chapman MS. Characterization of the capsid protein glycosylation of adeno-associated virus type 2 by high-resolution mass spectrometry. J Virol. 2006 Jun; 80(12):6171-6.
          View in: PubMed
        20. Fabiola F, Korostelev A, Chapman MS. Bias in cross-validated free R factors: mitigation of the effects of non-crystallographic symmetry. Acta Crystallogr D Biol Crystallogr. 2006 Mar; 62(Pt 3):227-38.
          View in: PubMed
        21. Korostelev A, Fenley MO, Chapman MS. Impact of a Poisson-Boltzmann electrostatic restraint on protein structures refined at medium resolution. Acta Crystallogr D Biol Crystallogr. 2004 Oct; 60(Pt 10):1786-94.
          View in: PubMed
        22. Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J. Study of the structural dynamics of the E coli 70S ribosome using real-space refinement. Cell. 2003 Jun 13; 113(6):789-801.
          View in: PubMed
        23. Lima S, Hildenbrand J, Korostelev A, Hattman S, Li H. Crystal structure of an RNA helix recognized by a zinc-finger protein: an 18-bp duplex at 1.6 A resolution. RNA. 2002 Jul; 8(7):924-32.
          View in: PubMed
        24. Fabiola F, Bertram R, Korostelev A, Chapman MS. An improved hydrogen bond potential: impact on medium resolution protein structures. Protein Sci. 2002 Jun; 11(6):1415-23.
          View in: PubMed
        25. Korostelev A, Bertram R, Chapman MS. Simulated-annealing real-space refinement as a tool in model building. Acta Crystallogr D Biol Crystallogr. 2002 May; 58(Pt 5):761-7.
          View in: PubMed
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