Formation of hybrid anthranilate synthetase in vitro from components of Aspergillus and Neurospora |
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Authors: | Etta Käfer J. A. DeMoss |
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Affiliation: | (1) Department of Biology, McGill University, Montreal, Quebec, Canada;(2) Department of Biology, San Diego University of California, La Jolla, California;(3) Present address: Biochemistry and Molecular Biology Group, University of Texas Medical School at Houston, Houston, Texas |
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Abstract: | Glutamine-dependent anthranilate synthetase was produced in vitro by mixing the extracts of a trypA and a trypC mutant of Aspergillus nidulans. Neither mutant alone possessed this activity. The enzyme formed in the mixture had the properties of the wild-type anthranilate synthetase which, together with N-(5-phosphoribosyl) anthranilate (PRA) isomerase and indole 3-glycerol phosphate (InGP) synthetase, is found in a 10S multienzyme complex. Extracts of the trypA69 mutant contained a 6.5S protein as the active component—presumably the trypC+ product—which in addition showed PRA isomerase and InGP synthetase activity. Extracts of the trypC801 mutant lacked all three enzyme activities but contained a 4.5S component—the trypA+ gene product—which in vitro showed ammonia-dependent anthranilate synthetase activity. These mutants are analogous in their properties to certain tryp-2 and tryp-1 mutants of Neurospora. When complementary extracts of the two genera were mixed (Aspergillus trypA with Neurospora tryp-1 or Aspergillus trypC with Neurospora tryp-2), a hybrid glutamine-dependent anthranilate synthetase was obtained which showed less than half the activity produced in homologous combinations.This study was supported by Grant GB 22655 from the National Science Foundation to J.A.DeM. |
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