A cloned tryptophan-synthesis gene from the Ascomycete Cochliobolus heterostrophus functions in Escherichia coli, yeast and Aspergillus nidulans

Turgeon, B. Gillian; Wd, MacRae; Rc, Garber; Gr, Fink; Oc, Yoder

doi:10.1016/0378-1119(86)90152-6

Cited by 28 publications

(5 citation statements)

References 15 publications

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“…For example, in A. nidulans, expression of trpC is significantly enhanced during conidiation; similarly, the level of the trpC transcript during growth in minimal medium is considerably higher than during growth in tryptophan-rich medium (32). In contrast, cultures of C. heterostrophus grown in minimal or in complete medium show no significant differences in the amount of TRPJ mRNA (31). In P. blakesleeanus, the TRPI mRNA did not appear to be regulated by light, which induces several developmental changes in this organism; it was also unaffected by the nutritional components of the culture.…”

Section: Resultsmentioning

confidence: 99%

“…In the context of this multifunctional trp gene, our nomenclature is expected to avoid confusion.) First, complementation of the phosphoribosyl anthranilate isomerase (trpF) and indoleglycerol phosphate synthase (trpC) activities of Escherichia coli by the corresponding functions of several fungi has been demonstrated (14,15,22,28,30,31). It was therefore reasonable to expect that the Phycomyces gene for TRPC and TRPF functions could also be selected in suitable E. coli strains.…”

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confidence: 99%

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Phycomyces blakesleeanus TRP1 gene: organization and functional complementation in Escherichia coli and Saccharomyces cerevisiae.

Revuelta¹,

Jayaram²

1987

Mol. Cell. Biol.

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We have cloned the gene encoding the TRPF and TRPC functions of Phycomyces blakesleeanus by complementation of the corresponding activities of Escherichia coli. TRPF also complemented a trpl mutation in Saccharomyces cerevisiae. As in other filamentous fungi, such as Neurospora and Aspergillus spp., the P. blakesleeanus TRPF and TRPC formed part of a trifunctional polypeptide encoded by a single gene (called TRP1). Transcription of TRP1 in P. blakesleeanus did not appear to be regulated by light or by the nutritional status of the culture. The information on the structure and organization of a P. blakesleeanus gene derived from these studies should be useful in devising molecular genetic strategies to analyze the sensory physiology of this organism.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Phycomyces blakesleeanus TRP1 gene: organization and functional complementation in Escherichia coli and Saccharomyces cerevisiae.

Revuelta¹,

Jayaram²

1987

Mol. Cell. Biol.

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“…Whereas S. cerevisiae exhibits a monofunctional PRA isomerase, the situation is different in other ascomycetes: several genes have been cloned that encode a trifunctional polypeptide with the arrangement NH2-glutamine amidotransferase-InGP synthase-PRA isomerase-COOH. Genes with this arrangement have been cloned from different fungi including N. crassa (167), A. nidulans (137), A. niger (105), Cochliobolus heterostrophus (195), Penicillium chrysogenum (166), and Phycomyces blakesleeanus (164). For the basidiomycete Schizophyllum commune a bifunctional NH2-InGP synthase-PRA isomerase-COOH was proposed (139).…”

Section: Tryptophan Branchmentioning

confidence: 99%

Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway.

Braus¹

1991

Microbiological Reviews

151

114

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“…The genes that encode PRAI activity in different filamentous fungi, including N. crassa (26), A. nidulans (31), Aspergillus niger (16), Cochliobolus heterostrophus (28), Schizophyllum commune (22), Penicillium chrysogenum (25), and Phycomyces blakesleeanus (24), have been cloned by complementation of the PRAI deficiency in E. coli trpC mutants. We therefore hypothesized that the A. parasiticus trpC gene could be selected in suitable E. coli mutant strains.…”

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confidence: 99%

Cloning and characterization of the trpC gene from an aflatoxigenic strain of Aspergillus parasiticus

Horng

Linz

Pestka

1989

Appl Environ Microbiol

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The trpC gene in the tryptophan biosynthetic pathway was isolated from an aflatoxigenic Aspergillus parasiticus by complementation of an Escherichia coli trpC mutant lacking phosphoribosylanthranilate isomerase (PRAI) activity. The cloned gene complemented an E. coli trpC mutant deficient in indoleglycerolphosphate synthase (IGPS) activity as well as an Aspergillus nidulans mutant strain that was defective in all three enzymatic activities of the trpC gene (glutamine amidotransferase, IGPS, and PRAI), thus indicating the presence of a complete and functional trpC gene. The location and organization of the A. parasiticus trpC gene on the cloned DNA fragment were determined by deletion mapping and by hybridization to heterologous DNA probes that were prepared from cloned trpC genes of A. nidulans and Aspergillus niger. These experiments suggested that the A. parasiticus trpC gene encoded a trifunctional polypeptide with a functional domain structure organized identically to those of analogous genes from other filamentous fungi. The A. parasiticus trpC gene was expressed constitutively regardless of the nutritional status of the culture medium. This gene should be useful as a selectable marker in developing a DNA-mediated transformation system to analyze the aflatoxin biosynthetic pathway of A. parasiticus.

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A cloned tryptophan-synthesis gene from the Ascomycete Cochliobolus heterostrophus functions in Escherichia coli, yeast and Aspergillus nidulans

Cited by 28 publications

References 15 publications

Phycomyces blakesleeanus TRP1 gene: organization and functional complementation in Escherichia coli and Saccharomyces cerevisiae.

Phycomyces blakesleeanus TRP1 gene: organization and functional complementation in Escherichia coli and Saccharomyces cerevisiae.

Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway.

Cloning and characterization of the trpC gene from an aflatoxigenic strain of Aspergillus parasiticus

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