• Title of article

    Maize Seryl-tRNA Synthetase: Specificity of Substrate Recognition by the Organellar Enzyme

  • Author/Authors

    Rokov-Plavec، نويسنده , , Jasmina and Lesjak، نويسنده , , Sonja and Landeka، نويسنده , , Irena and Mijakovic، نويسنده , , Ivan and Weygand-Durasevic، نويسنده , , Ivana، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2002
  • Pages
    11
  • From page
    40
  • To page
    50
  • Abstract
    In our study of seryl-tRNA formation in maize, we investigated the enzymes involved in serylation. Only two dissimilar seryl-tRNA synthetase (SerRS) cDNA clones were identified in the Zea mays EST (expressed sequence tag) databases. One encodes a seryl-tRNA synthetase, which presumably functions in the organelles (SerZMm), while the other synthetase product is more similar to eukaryotic cytosolic counterparts (SerZMc). The expression of SerZMm in Saccharomyces cerevisiae resulted in complementation of mutant respiratory phenotype, caused by a disruption of the nuclear gene, presumably encoding yeast mitochondrial seryl-tRNA synthetase (SerSCm). Purified mature SerZMm displays tRNA-assisted serine activation and aminoacylates maize mitochondrial and chloroplast tRNASer transcripts with similar efficiencies, raising the possibility that only two isoforms of seryl-tRNA synthetase may be sufficient to catalyze seryl-tRNASer formation in three cellular compartments of Zea mays. Phylogenetic analysis suggests that SerZMm is of mitochondrial origin.
  • Keywords
    seryl-tRNA synthetases , organelles , tRNA-dependent amino acid recognition , complementation , Zea mays
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    2002
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1618889