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Pregled bibliografske jedinice broj: 45349

Maize seryl-tRNA synthetase: specificity of substrate recognition by the organellar enzyme


Rokov-Plavec, Jasmina; Lesjak, Sonja; Landeka, Irena; Mijaković, Ivan; Weygand-Đurašević, Ivana
Maize seryl-tRNA synthetase: specificity of substrate recognition by the organellar enzyme // Archives of Biochemistry and Biophysics, 397 (2002), 1; 40-50 (međunarodna recenzija, članak, znanstveni)


Naslov
Maize seryl-tRNA synthetase: specificity of substrate recognition by the organellar enzyme

Autori
Rokov-Plavec, Jasmina ; Lesjak, Sonja ; Landeka, Irena ; Mijaković, Ivan ; Weygand-Đurašević, Ivana

Izvornik
Archives of Biochemistry and Biophysics (0003-9861) 397 (2002), 1; 40-50

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Seryl-tRNA synthetases; organelles; Zea mays; tRNA-dependent amino acid recognition; horizontal gene transfer

Sažetak
In our study of seryl-tRNA formation in maize, we characterized the enzymes involved in serylation. Only two dissimilar seryl-tRNA synthetase (SerRS) cDNA clones were identified in the Zea mays EST databases. One encodes a seryl-tRNA synthetase which presumably functions in the organelles, while the other synthetase product is more similar to eukaryotic cytosolic counterparts. We analyzed the specificity and the mechanism of substrate recognition by purified overexpressed organellar SerRS. This enzyme displays tRNA-dependent serine activation and aminoacylates maize mitochondrial and chloroplast tRNASer transcripts with similar efficiences, which may suggest that only two isoforms of seryl-tRNA synthetase are sufficient to catalyze seryl-tRNASer formation in three cellular compartments of Zea mays.

Izvorni jezik
Engleski

Znanstvena područja
Biologija



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  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE