Biopolym. Cell. 1999; 15(5):409-414.
http://dx.doi.org/10.7124/bc.000538
Structure and Function of Biopolymers
Cytoplasmic and nuclear localization of tyrosyl-tRNA synthetase in higher eukaryotic cells studied by immunoelectronic microscopy
1Ribkinska T. A., 2Ivanova Ju. L., 2Cherny N. E., 2Popenko V. I., 1Matsuka G. Kh., 1Kornelyuk A. I.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences
    32, Vavilova Str., Moscow, Russian Federation, 119991

Abstract

The localization of tyrosyl-tRNA synthetase has been studied by immunoelectronic microscopy in bovine kidney cells and fibroblasts of RAT I line which have been treated by monoclonal antibodies T3 raised against bovine tyrosyl-tRNA synthetase an by complexes of protein A-colloidal gold. The localization of tyrosyl-tRNA synthetase har been revealed both in cytoplasm and in the nucleus of mammalian cells. Tyrosyl-tRNA synthetase is located in cytoplasm mainly in the vicinity of polyribosomes what supports the compartmentatization conception of the components of protein synthesis apparatus. A significant portion of synthetase detected in the nucleus is located mainly in the region of diffuse chromatin, and partly in the nudeolus. In general, localization of tyrosyl-tRNA synthetase in mammalian cells is very similar to the localization of p43 protein of codosome, a precursor of the EMAP II cytokine, which is highly homologous to the non-catalytic C-terminal domain of tyrosyl-tRNA synthetase. Nuclear localization of tyrosyl-tRNA synthetase implies that this enzyme is involved in some non-canonical functions in the nucleus of eukaryotic cell. It is possible that this function may be related to the export of mature tRNA from nucleus to cytoplasm.
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