Nina Moor

Summary

Affiliation: Institute of Chemical Biology and Fundamental Medicine
Country: Russia

Publications

  1. ncbi request reprint Interaction of human phenylalanyl-tRNA synthetase with specific tRNA according to thiophosphate footprinting
    I A Vasil'eva
    Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, Russia
    Biochemistry (Mosc) 74:175-85. 2009
  2. ncbi request reprint tRNA discrimination by T. thermophilus phenylalanyl-tRNA synthetase at the binding step
    Inna A Vasil'eva
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Russia
    J Mol Recognit 15:188-96. 2002
  3. ncbi request reprint Effect of nucleotide replacements in tRNAPhe on positioning of the acceptor end in the complex with phenylalanyl-tRNA synthetase
    I A Vasil'eva
    Institute of Chemical Biology and Fundamental Medicine, Siberian Division, Russian Academy of Sciences, Novosibirsk 630090, Russia
    Biochemistry (Mosc) 69:154-63. 2004
  4. ncbi request reprint Interaction of aminoacyl-tRNA synthetases with tRNA: general principles and distinguishing characteristics of the high-molecular-weight substrate recognition
    N A Moor
    Institute of Chemical Biology and Fundamental Medicine, Siberian Division of the Russian Academy of Sciences, Novosibirsk, Russia
    Biochemistry (Mosc) 72:247-63. 2007
  5. ncbi request reprint Affinity modification of phenylalanyl-tRNA synthetase from Thermus thermophilus by tRNAPhe transcripts containing 4-thiouridine
    N A Moor
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia
    Biochemistry (Mosc) 63:1044-50. 1998
  6. ncbi request reprint Localization of the binding site for the 3'-terminal sequence of tRNAPhe in subunits of phenylalanyl-tRNA synthetase from Thermus thermophilus
    N A Moor
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia
    Biochemistry (Mosc) 63:1051-6. 1998
  7. ncbi request reprint Determination of tRNA(Phe) nucleotides contacting the subunits of Thermus thermophilus phenylalanyl-tRNA synthetase by photoaffinity crosslinking
    N A Moor
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk 630090, Russia
    Biochim Biophys Acta 1518:226-36. 2001
  8. ncbi request reprint Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end
    Nina Moor
    Novosibirsk Institute of Bioorganic Chemistry, 630090 Novosibirsk, Russia
    Biochemistry 42:10697-708. 2003
  9. ncbi request reprint The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end
    Nina Moor
    Institute of Chemical Biology and Fundamental Medicine, 630090 Novosibirsk, Russia
    Biochemistry 45:10572-83. 2006
  10. doi request reprint Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNA(Phe) with 3,4-dihydroxy-L-phenylalanine
    Nina Moor
    Institute of Chemical Biology and Fundamental Medicine, 630090 Novosibirsk, Russia
    Chem Biol 18:1221-9. 2011

Collaborators

  • O I Lavrik
  • I A Vasil'eva
  • Liron Klipcan
  • Inna Levin
  • Mark Safro
  • Naama Kessler
  • Olga Kotik-Kogan
  • Inna A Vasil'eva
  • E A Semenova
  • Igal Finarov
  • Linda Spremulli
  • Paul Templeton
  • Emine Koc
  • Dmitry Tworowski
  • A Favre
  • Valentina N Ankilova

Detail Information

Publications14

  1. ncbi request reprint Interaction of human phenylalanyl-tRNA synthetase with specific tRNA according to thiophosphate footprinting
    I A Vasil'eva
    Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, Russia
    Biochemistry (Mosc) 74:175-85. 2009
    ..The data indicate that mechanisms of interaction between phenylalanyl-tRNA synthetases and specific tRNAs are different in prokaryotes and eukaryotes...
  2. ncbi request reprint tRNA discrimination by T. thermophilus phenylalanyl-tRNA synthetase at the binding step
    Inna A Vasil'eva
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Russia
    J Mol Recognit 15:188-96. 2002
    ..The highest affinity of T. thermophilus PheRS for cognate tRNA, observed for synthetase-tRNA complexes, results in 100-3000-fold binding discrimination against non-cognate tRNAs...
  3. ncbi request reprint Effect of nucleotide replacements in tRNAPhe on positioning of the acceptor end in the complex with phenylalanyl-tRNA synthetase
    I A Vasil'eva
    Institute of Chemical Biology and Fundamental Medicine, Siberian Division, Russian Academy of Sciences, Novosibirsk 630090, Russia
    Biochemistry (Mosc) 69:154-63. 2004
    ..The main recognition elements of tRNA(Phe), which optimize its initial binding with PheRS, are also involved in generation of the catalytically active complex providing functional conformation of the acceptor arm...
  4. ncbi request reprint Interaction of aminoacyl-tRNA synthetases with tRNA: general principles and distinguishing characteristics of the high-molecular-weight substrate recognition
    N A Moor
    Institute of Chemical Biology and Fundamental Medicine, Siberian Division of the Russian Academy of Sciences, Novosibirsk, Russia
    Biochemistry (Mosc) 72:247-63. 2007
    ..Diversity and identity of biochemical functions of the recognition elements make substantial contribution to the specificity of such interactions...
  5. ncbi request reprint Affinity modification of phenylalanyl-tRNA synthetase from Thermus thermophilus by tRNAPhe transcripts containing 4-thiouridine
    N A Moor
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia
    Biochemistry (Mosc) 63:1044-50. 1998
    ..The prevalence of modification of the alpha-subunit suggests that tRNA has contacts with the enzyme, which have not been deciphered previously by X-ray analysis...
  6. ncbi request reprint Localization of the binding site for the 3'-terminal sequence of tRNAPhe in subunits of phenylalanyl-tRNA synthetase from Thermus thermophilus
    N A Moor
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia
    Biochemistry (Mosc) 63:1051-6. 1998
    ..These data suggest that the nucleotide found at position 75 of tRNAPhe interacts with the beta-subunit of phenylalanyl-tRNA synthetase...
  7. ncbi request reprint Determination of tRNA(Phe) nucleotides contacting the subunits of Thermus thermophilus phenylalanyl-tRNA synthetase by photoaffinity crosslinking
    N A Moor
    Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk 630090, Russia
    Biochim Biophys Acta 1518:226-36. 2001
    ..The data of independent biochemical approaches strongly suggest conformational flexibility of the complex under functional conditions, thus reflecting the importance of macromolecular dynamics for the interaction...
  8. ncbi request reprint Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end
    Nina Moor
    Novosibirsk Institute of Bioorganic Chemistry, 630090 Novosibirsk, Russia
    Biochemistry 42:10697-708. 2003
    ....
  9. ncbi request reprint The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end
    Nina Moor
    Institute of Chemical Biology and Fundamental Medicine, 630090 Novosibirsk, Russia
    Biochemistry 45:10572-83. 2006
    ..Our data suggest that the idiosyncratic feature of PheRS, which aminoacylates the 2'-OH group of the terminal ribose, is dictated by the system-specific topology of the CCA end-binding site...
  10. doi request reprint Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNA(Phe) with 3,4-dihydroxy-L-phenylalanine
    Nina Moor
    Institute of Chemical Biology and Fundamental Medicine, 630090 Novosibirsk, Russia
    Chem Biol 18:1221-9. 2011
    ..However, editing activity of PheRS does not guarantee reduction of the aminoacylation error rate to escape misincorporation of L-dopa into polypeptide chains...
  11. pmc Purification, crystallization and preliminary X-ray characterization of a human mitochondrial phenylalanyl-tRNA synthetase
    Inna Levin
    Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel
    Acta Crystallogr Sect F Struct Biol Cryst Commun 63:761-4. 2007
    ..The crystals diffracted to 2.2 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 55, b = 90, c = 96 A...
  12. doi request reprint The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase
    Liron Klipcan
    Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel
    Structure 16:1095-104. 2008
    ..Thus, formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement (hinge-type rotation through approximately 160 degrees) of the ABD upon tRNA binding...
  13. ncbi request reprint Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes
    Nina Moor
    Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
    Protein Expr Purif 24:260-7. 2002
    ..coli is five times higher...
  14. ncbi request reprint Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase
    Olga Kotik-Kogan
    Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel
    Structure 13:1799-807. 2005
    ..Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system...