An asparaginase of Aspergillus nidulans is subject to oxygen repression in addition to nitrogen metabolite repression |
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Authors: | Patricia M Shaffer Herbert N Arst Jr Leah Estberg Leon Fernando Tran Ly and Mark Sitter |
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Institution: | (1) Department of Chemistry, University of San Diego, 92110 San Diego, CA, USA;(2) Department of Bacteriology, Royal Postgraduate Medical School, Hammersmith Hospital, Ducane Road, W12 OHS London, UK |
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Abstract: | Summary Of five amidohydrolase activities subject to nitrogen metabolite repression in Aspergillus nidulans, l-asparaginase shows clearest evidence of also being subject to repression by atmospheric oxygen. Such oxygen repressibility is only evident under nitrogen metabolite derepressed conditions. Asparaginase levels are also considerably elevated by areA300, an altered function allele of the positive acting wide domain regulatory gene areA mediating nitrogen metabolite repression and are drastically reduced by loss of function mutations in areA. A. nidulans has two l-asparaginase enzymes and it has been shown by the use of appropriate mutants that these regulatory effects are exerted on the expression of that specified by the ahrA gene but probably not that specified by the apnA gene.
Present address: (until 25 August, 1988) Department of Genetics, University of Georgia, Athens, GA 30602, USA |
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Keywords: | Amidohydrolase Asparaginase Aspergillus nidulans Nitrogen metabolite repression Oxygen repression |
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