Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe.
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.
Eden
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Department of Genetics, Hebrew University of Jerusalem, Givat-Ram, Israel.
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D000595:Amino Acid Sequence; D000597:Amino Acids, Branched-Chain / Q000378:metabolism*; D001483:Base Sequence; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D012568:Schizosaccharomyces / Q000201:enzymology* / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D000637:Transaminases / Q000737:chemistry* / Q000235:genetics
D000597:Amino Acids, Branched-Chain; D000637:Transaminases; C019798:branched-chain-amino-acid transaminase