Biopolym. Cell. 2007; 23(2):130-136.
Molecular Biophysics
Conformational mobility investigation of tyrosyl-tRNA synthetase C-module and its complex with tRNA using the methods of time-resolved fluorescence spectroscopy
1Kordysh M. O., 1Kyryushko G. V., 2Mely Y., 1Kornelyuk O. I.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Universite de Strasbourg
    4, rue Blaise Pascal, Strasbourg, France, F-67081


The non-catalytic C-module of mammalian tyrosyl-tRNA synthetase displays both RNA-binding ability and cytokine activity. C-module contains a unique tryptophan residue (Trpl44), located out of RNA-binding site and a conservative aromatic residue Phe127 located inside of its RNA-binding site. Phe127 was replaced by fluorophore Trp 127 using the method of site-directed mutagenesis. The interaction of C-module with tRNA was investigated by time-resolved fluorescence spectroscopy. Obtained fluorescence decay parameters of Trp144 and Trp127 of C-module and its complex with tRNA are characterized by the additional short-lived component without any significant changing of other fluorescence parameters in the presence of nucleic acid. These data indicate the existence of the polymorphism of Trp 127 microenvironment that is conditioned by the dynamic protein-nucleic acid interaction mechanism.
Keywords: tyrosyl-tRNA synthetase C-module, time-resolved fluorescence spectroscopy, conformational mobility.


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