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
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