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Citation
Kerjan, P., Cerini, C., Semeriva, M., Mirande, M. (1994). The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals.  Biochim. Biophys. Acta 1199(3): 293--297.
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FBrf0073545
Publication Type
Research paper
Abstract

In all mammalian cells studied so far, a multienzyme complex containing the nine aminoacyl-tRNA synthetases specific for the amino acids Glu, Pro, Ile, Leu, Met, Gln, Lys, Arg and Asp was characterized. The complexes purified from various sources display very similar polypeptide compositions; they are composed of 11 polypeptides with molecular masses ranging from 18 to 150 kDa. By contrast, the corresponding enzymes from prokaryotes and lower eukaryotes behave as free enzymes. In order to test for the ubiquity of the multisynthetase complex in all metazoan species, we have searched for a similar complex in Drosophila. We have purified to homogeneity, from Schneider cells, a high molecular weight complex comprising the same nine synthetase activities. Its polypeptide composition resembles that of the complexes isolated from mammalian sources. By using the Western blotting procedure, some of the constituent polypeptides of the Drosophila complex were assigned to specific aminoacyl-tRNA synthetases. These findings support the proposal according to which the multisynthetase complex is an idiosyncratic feature of all higher eukaryotic cells.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Biochim. Biophys. Acta
    Title
    Biochimica et Biophysica Acta
    Publication Year
    1947-
    ISBN/ISSN
    0006-3002
    Data From Reference
    Genes (8)