Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe

Amir Eden, Nissim Benvenisty*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The Saccharomyces cerevisiae genes for the cytosolic and mitochondrial branched-chain amino-acid aminotransferases (BCAT) were isolated recently. These genes show significant homology to mammalian ECA39, originally isolated as a gene regulated by the c-myc oncogene. We now report the isolation of the Schizosaccharomyces pombe eca39/BCAT gene. The S. pombe protein shows 47-52% identity to other eukaryotic BCAT proteins isolated from S. cerevisiae, nematode, mouse and man. A genetic growth assay for BCAT activity was established using an S. cerevisiae strain disrupted in both BCAT isoenzymes. Consequently, the activity of the S. pombe BCAT was demonstrated by genetic and biochemical means. Possible applications of BCAT-encoding genes as selection markers in yeast transformation are proposed. The sequence has been deposited in the GenBank data library under Accession Number U88029.

Original languageAmerican English
Pages (from-to)189-194
Number of pages6
JournalYeast
Volume14
Issue number2
DOIs
StatePublished - 30 Jan 1998

Keywords

  • Aminotransferase
  • Branched-chain amino acids
  • Saccharomyces cerevisiae
  • Schizosaccharomyces pombe

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