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

Revuelta, José Luis; Jayaram, Makkuni

doi:10.1128/mcb.7.8.2664

Cited by 21 publications

(7 citation statements)

References 30 publications

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“…These data also showed that a 280-bp HindIII-BamHI fragment located at the 3' end of the insert was necessary for PRAI activity. This result, together with the inferences that both a 930-bp HindIII-XhoI fragment on pJH34 (see previous section) and a minimum of 2.3 kb are necessary for the complete trpC function in filamentous fungi (5,17,21,(24)(25)(26), suggested that the A. parasiticus trpC transcript was initiated near the 3' end of the 930-bp HindIII-XhoI fragment and terminated within the 280-bp HindIII-BamHI fragment (Fig. 3, longer arrow on plasmid pJH34).…”

Section: Resultssupporting

confidence: 60%

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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Section: Resultssupporting

confidence: 60%

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 sequences were derived from E. coli (gwec: Horowitz et al, 1983). Salmonella typhimurium (gwebt: Horowitz et al, 1983), Phycomyces blakesleeanus (pbtrpl: Revuelta and Jayaram, 1987), Aspergillus nidulans (antrpl: Mullaney et al, 1985), Neurospora crassa (nnnc2: Schechtman and Yanofsky, 1983), S. cerevisiae (isbyn: Tschumper and Carbon, 1980) and K . Iactis (kltrpl: this work).…”

Section: The K Lactis Ipp Genementioning

confidence: 99%

“…In microorganisms, the biosynthesis of tryptophan from chorismate involves a five-step pathway (Crawford, 1975), the third reaction of which is catalysed by the enzyme N-(5'-phosphoribosyl) anthranilate isomerase (PRA isomerase). In filamentous fungi, this activity is associated with a trifunctional polypeptide which also catalyses two other steps in tryptophan biosynthesis (Schechtman and Yanofsky, 1983;Mullaney et ul., 1985;Revuelta and Jayaram, 1987), while in bacteria it is part of a similar bifunctional enzyme (Crawford, 1975;Horowitz e f ul., 1983). However, in the yeast Succhuromyces cerevisiue PRA isomerase is encoded independently of the other tryptophan biosynthetic enzymes by the TRPl gene (Tschumper and Carbon, 1980).…”

Section: Introductionmentioning

confidence: 99%

Cloning and analysis of the Kluyveromyces lactis TRP1 gene: A chromosomal locus flanked by genes encoding inorganic pyrophosphatase and histone H3

Stark

Milner

1989

Yeast

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The TRP1 gene of the yeast Kluyveromyces lactis has been cloned from a genomic library by complementation of the Saccharomyces cerevisiae trp1-289 mutation. The gene was located within the clone by transposon mutagenesis and the coding region identified by DNA sequencing. This has indicated that K. lactis TRP1 encodes a 210-amino acid polypeptide which shows 53% identity to the homologous S. cerevisiae protein. The K. lactis TRP1 gene has been disrupted by substituting the S. cerevisiae URA3 gene for a large part of the TRP1 coding sequence. Replacement of the chromosomal TRP1 locus with this construction has enabled the production of non-reverting trp1- strains of K. lactis, while a genetic analysis of the disrupted allele confirmed that the TRP1 gene had been cloned. DNA sequencing has also shown that the K. lactis TRP1 sequence is flanked by genes encoding inorganic pyrophosphatase and histone H3, which we have designated IPP and HHT1 respectively. Hybridization studies have shown that in common with S. cerevisiae, K. lactis has two copies of the histone H3 gene. Each H3 gene is closely linked to a gene encoding histone H4 and in both yeast species the IPP gene is tightly linked to one of the histone gene pairs.

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“…Tri‐functional tryptophan genes 1 have been cloned from diverse filamentous fungi including several ascomycetes, the basidiomycetes Coprinus bilanatus TRP2 [4], Coprinus cinereus trp2 [5], Flammulina velutipes TRP1 [6], Phanerochaete chrysosporium trpC [7], Schizophyllum commune TRP1 [8] and the zygomycete Phycomyces blakesleeanus TRP1 [9]. Several of these genes have been used to develop transformation systems and some have been expressed in heterologous hosts [5].…”

Section: Introductionmentioning

confidence: 99%

Agaricus bisporusandCoprinus bilanatus TRP2genes are tri-functional with conserved intron and domain organisations

Challen¹,

Zhang²,

Elliott³

2002

FEMS Microbiology Letters

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Cloned homobasidiomycete TRP2 genes for Agaricus bisporus and Coprinus bilanatus were sequence-characterised. Both genes encode tri-functional proteins with activity domains for glutamine amidotransferase (GAT; G domain), indole glycerol phosphate synthase (InGP; C domain) and phosphoribosyl anthranilate isomerase (F domain). A conserved intron disrupts the GAT-coding sequence in both genes. Consensus amino acid (aa) signatures were identified for GAT and InGP, but in the latter 15-aa signature, one residue did not fit the previously defined consensus. Protein architecture and parsimony analysis with analogous proteins indicate domain organisation (NH(2)-G-C-F-COOH) was as for other filamentous fungi. The data do not support earlier suggestions that the three activity domains are detached in A. bisporus.

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

Cited by 21 publications

References 30 publications

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

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

Cloning and analysis of the Kluyveromyces lactis TRP1 gene: A chromosomal locus flanked by genes encoding inorganic pyrophosphatase and histone H3

Agaricus bisporusandCoprinus bilanatus TRP2genes are tri-functional with conserved intron and domain organisations

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