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Identification of an apparent aminoacyl-tRNA synthetase activator factor as tRNA nucleotidyltransferase

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Summary

The ability of yeast extracts to aminoacylate crude yeast tRNA with leucine and other amino acids is largely lost after chromatography of the extracts in DEAE-Sephadex. The original aminoacylating ability is restored by combining protein fractions from the DEAE-chromatogram. The characteristics of this reactivation are very similar to the activation, by protein factors, of certain aminoacyl-tRNA synthetases reported by others. The results in this work indicate that the apparent aminoacyl-tRNA synthetase activator factor is the tRNA nucleotidyltransferase and that the restoration of the original tRNA aminoacylating ability is a consequence of the repairing of the 3' end of incomplete tRNA chains.

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Authors and Affiliations

  1. Instituto de Enzimología y Patologia Molecular del Consejo Superior de Investigaciones Cientificas, Facultad de Medicina de la Universidad Autónoma, Madrid-34, Spain

    José M. del Rio & Claudio F. Heredia

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  1. José M. del Rio
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  2. Claudio F. Heredia
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del Rio, J.M., Heredia, C.F. Identification of an apparent aminoacyl-tRNA synthetase activator factor as tRNA nucleotidyltransferase. Mol Cell Biochem 50, 101–106 (1983). https://doi.org/10.1007/BF00285636

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  • DOI: https://doi.org/10.1007/BF00285636

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