An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant.
A cDNA encoding a glutamine amidotransferase and cyclase catalyzing the fifth and sixth steps of the histidine (His) biosynthetic pathway has been isolated from Arabidopsis thaliana. The N- and C-terminal domains of the primary structure deduced from a full-length Arabidopsis hisHF (At-HF) cDNA showed significant homology to the glutamine amidotransferase and cyclase of microorganisms, respectively. Effective suppression of the His auxotrophy of a Saccharomyces cerevisiae his7 mutant with the At-HF cDNA confirmed that the At-HF protein has bifunctional glutamine amidotransferase (HisH) and cyclase (HisF) activities.
Fujimori
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K
Takarazuka Research Institute, Novartis Pharma K.K., Japan.
Ohta
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D
D000595:Amino Acid Sequence; D000619:Aminohydrolases; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006639:Histidine / Q000378:metabolism*; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D016366:Open Reading Frames; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000254:growth & development*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014166:Transferases / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*
D018076:DNA, Complementary; D009097:Multienzyme Complexes; D011994:Recombinant Proteins; D006639:Histidine; D014166:Transferases; C087227:imidazole glycerol phosphate synthase; D000619:Aminohydrolases