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  • 1
    Electronic Resource
    Electronic Resource
    Comparison and cross-species expression of the acetyl-CoA synthetase genes of the ascomycete fungi, Aspergillus nidulans and Neurospora crassa (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The genes encoding the acetate-inducible enzyme acetyl-coenzyme A synthetase from Neurospora crassa and Aspergillus nidulans (acu-5 and facA, respectively) have been cloned and their sequences compared. The predicted amino acid sequence of the Aspergillus enzyme has 670 amino acid residues and that of the Neurospora enzyme either 626 or 606 residues, depending upon which of the two possible initiation codons is used. The amino acid sequences following the second alternative AUG show 86% homology between the two species; the extended N-terminal sequences show no homology. The Neurospora protein is characterized by the appearance of the S(T)PXX sequence motif where the amino acid homologies break down. The codon usage is biased in both genes, with a marked deficiency, especially in Neurospora, of codons with A in the third position.The facA transcribed sequence contains six introns: one in the long leader sequence, one in the 5′ coding sequence not homologous with acu-5, and four within the sequence that is largely similar to that of acu-5. Only one intron, corresponding in size and position to the furthest downstream of the facA introns, is found in acu-5. The evolution of introns during the divergence of these two Ascomycete fungi is discussed. Each of the two genes has been transferred by transformation into the other species. Each species is evidently able to splice out the other's introns. Most transformants have normal acetate-induction of acetyl-CoA synthetase, emptying that the two genes respond to transcriptional control signals common to both species, in spite of the striking divergence of their 5′ ends.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1990.tb00611.x
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  • 2
    Electronic Resource
    Electronic Resource
    The acetate regulatory gene facB of Aspergillus nidulans encodes a Zn(II)2Cys6 transcriptional activator (1997)
    Springer
    Molecular genetics and genomics 254 (1997), S. 495-504 
    Details
    ISSN: 1617-4623
    Keywords: Key words Acetate metabolism  ;  facB  ;  Zn(II)2Cys6 (C6 zinc) binuclear cluster  ;  Aspergillus  ;  Gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Genetic studies have indicated that the facB gene of Aspergillus nidulans is a major regulatory gene involved in acetamide and acetate utilisation. Sequencing of the facB gene revealed that it encodes a protein that contains an N-terminal GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster for DNA binding, leucine zipper-like heptad repeat motifs and central and C-terminal acidic α-helical regions, consistent with a function as a DNA-binding transcriptional activator. The Zn(II)2Cys6 cluster shows strong similarity with those of the Saccharomyces cerevisiae carbon metabolism regulatory proteins CAT8 and SIP4. A significant level of similarity with CAT8 is found throughout the length of the protein, suggesting at least partial functional homology. The facB genes of Aspergillus oryzae and Aspergillus niger were also sequenced and found to be highly conserved. Deletion of the facB gene confirmed that it is required for growth on acetate as a sole carbon source. Functional dissection using deletion and fusion constructs and in vitro mutagenesis indicated that the Zn(II)2Cys6 cluster and the C-terminal end of the protein are required for function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050444
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  • 3
    Electronic Resource
    Electronic Resource
    The Aspergillus nidulans CCAAT-binding factor AnCP/AnCF is a heteromeric protein analogous to the HAP complex of Saccharomyces cerevisiae (1998)
    Springer
    Molecular genetics and genomics 257 (1998), S. 404-411 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsAspergillus ; CCAAT ; HapC ; Hap complex ; DNA binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Aspergillus nidulans hapC gene was expressed as a fusion protein with MalE or glutathione-S-transferase (GST) in Escherichia coli, and used for the purification of HapC and the preparation of anti-HapC antiserum. The CCAAT-binding factor AnCP/AnCF contains a component with an approximate molecular mass of 32 kDa that cross-reacts with the antibody. The MalE-HapC fusion protein was able to replace authentic HapC in AnCP when incubated under appropriate conditions. Furthermore, reconstitution experiments with recombinant HapC, yHAP2 and yHAP5 polypeptides showed that all three polypeptides were required for the assembly of a complex capable of binding to CCAAT-containing taaG2 promoter DNA. The relationship between AnCP/AnCF and the Saccharomyces cerevisiae HAP complex is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050664
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  • 4
    Electronic Resource
    Electronic Resource
    A cis -dominant regulatory mutation affecting enzyme induction in the enkaryote Aspergillus nidulans (1975)
    [s.l.] : Nature Publishing Group
    Nature 253 (1975), S. 210-212 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] In Aspergillus nidulans, lesions in the gene areA can result in inability to utilise a wide variety of nitrogen sources, including acetamide9. This gene is probably involved in regulation of enzyme synthesis by ammonium (ref. 9 and M.J.H., unpublished). Strains containing the mutation, areA2U9 grow ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/253210a0
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  • 5
    Electronic Resource
    Electronic Resource
    Multiple copies of the amdS gene of Aspergillus nidulans cause titration of trans-acting regulatory proteins (1987)
    Springer
    Current genetics 12 (1987), S. 21-31 
    Details
    ISSN: 1432-0983
    Keywords: Aspergillus nidulans ; Transformation ; Gene regulation ; Acetamidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary It has been established that a plasmid containing the amdS gene of Aspergillus nidulans may be used to transform amdS+ strains by selecting for increased utilization of acetamide as sole nitrogen source. Analysis of transformants has shown that multiple tandem copies of the plasmid can be integrated into the chromosome, commonly at sites other than the amdS locus. While the transformed phenotype was relatively stable through mitotic and meiotic divisions evidence was found for variation in plasmid copy number presumably due to unequal recombination events. Expression of the integrated amdS genes was related to copy number, and the amdS RNA produced was similar in size to wild-type RNA. Evidence for titration of the product of the regulatory gene amdR by multiple copies of amdS was found. No titration of the product of the areA gene was observed, and amdS expression was still dependent on areA function. Multiple copies of the amdI9 mutation resulted in poor growth on acetate. This was not observed in the case of the amdS+ gene. The cis-acting amdI9 mutation causes increased facB dependent acetate induction of amdS expression. Titration of the facB gene produce by amdI9 DNA, but not by amdS+ DNA, therefore suggested that the mutation results in increased affinity for the facB gene product.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00420723
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  • 6
    Electronic Resource
    Electronic Resource
    Pleiotropic mutants affecting the control of nitrogen metabolism in Aspergillus nidulans (1973)
    Springer
    Molecular genetics and genomics 125 (1973), S. 99-107 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants of Aspergillus nidulans with lesions in gene amdT are pleiotropically affected in their ability to utilize a wide variety of nitrogen sources in the presence of glucose. Ability to utilize a number of these compounds as sole sources of carbon and nitrogen is not altered. One of these mutants, amdT102, has properties consistent with it being derepressed for glucose repression of the utilization of most (but not all) nitrogen sources. The amdT102 mutant can grow strongly on histidine, lysine and cystine as sole nitrogen sources while the wild type strain grows extremely poorly on these amino acids. Similar but less extreme effects apply to many other nitrogen sources. The amdT19 mutant is unable to utilize most nitrogen sources in the presence of glucose, suggesting that it is subject to greatly increased repression of nitrogen source utilization. The amdT mutants are not affected in their ability to use many compounds as sole carbon sources. Carbon sources other than glucose also affect utilization of nitrogen sources in the amdT mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268862
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  • 7
    Electronic Resource
    Electronic Resource
    The genetic analysis of regulation of amidase synthesis inAspergillus nidulans (1970)
    Springer
    Molecular genetics and genomics 108 (1970), S. 107-116 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A mutantfmdS-1, lacking formamidase activity and unable to use formamide as a nitrogen source, has been isolated inAspergillus nidulans. The properties of the mutant suggest thatfmdS is the structural gene for the formamidase. Among mutants resistant to fluoroacetamide, classes with reduced ability to grow on acetamide have been found. One class (amdS −) lack acetamidase activity and are recessive. TheamdS locus is on linkage group III and recombines freely withfmdS, which is also on linkage group III. Another class (amdR −) grow poorly on acetamide and are probably allelic to the constitutiveamdR c mutants. Two types ofamdR − mutants occur. One produces low acetamidase levels under all conditions. The other produces low acetamidase and formamidase under conditions where ammonia repression can operate, but normal levels where repression cannot occur.amdR − mutants are recessive toamdR + andamdR c alleles. It is suggested that theamdR locus is involved in positive control and also in ammonia repression of amidase synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02430517
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  • 8
    Electronic Resource
    Electronic Resource
    The genetic analysis of regulation of amidase synthesis inAspergillus nidulans (1970)
    Springer
    Molecular genetics and genomics 108 (1970), S. 97-106 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Aspergillus nidulans uses an acetamidase enzyme to grow on acetamide as a carbon or as a nitrogen source. Acrylamide is a substrate for the enzyme but does not induce its synthesis. Mutants capable of growing on acrylamide as a nitrogen source have been isolated. Two classes of mutant have been found —amdR c mutants on linkage group II andamdT c on linkage group III.amdR c mutants produce high constitutive acetamidase levels. The enzyme is still inducible by amides, but to a lesser extent than wild type, and is still subject to repression by ammonia and by carbon metabolites derived from glucose.amdR c mutants are semi-dominant to the wild type allele in heterozygous, diploids. TheamdT c mutant is not subject to carbon metabolite repression, of the acetamidase. The enzyme is inducible by amides and repressible by ammonia. TheamdT c mutation also results in reduced ability to grow on formamide as a nitrogen source and to lowered levels of a second amidase enzyme.amdT c is semi-dominant in heterozygous diploids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02430516
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  • 9
    Electronic Resource
    Electronic Resource
    Repression of enzymes of nitrogen catabolism by methylammonium and caesium chloride in strains of Aspergillus nidulans insensitive to ammonium repression (1974)
    Springer
    Molecular genetics and genomics 132 (1974), S. 147-152 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Growth of Aspergillus nidulans in the presence of methylammonium leads to lowered levels of the enzymes, acetamidase, formamidase, benzamidase, histidase, nitrate reductase and urate oxidase. This phenomenon is not altered in strains that are insensitive to ammonium repression due to a lesion in the gdhA gene. Similarly repression of acetamidase, formamidase and histidase by high concentrations of caesium ion is not affected in these strains. The results indicate that caesium ion and methylammonium may not act as direct analogues of ammonium in repression of enzyme synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272180
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  • 10
    Electronic Resource
    Electronic Resource
    Pleiotropic mutants ofAspergillus nidulans altered in carbon metabolism (1977)
    Springer
    Molecular genetics and genomics 150 (1977), S. 193-204 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants altered in carbon catabolite regulation have been isolated by selecting for mutants of theareA217 strain capable of using acetamide as the sole nitrogen source in the presence of sucrose. In addition tocreA mutants described previously by Arst and Cove, strains with mutations in two new genes,creB andcreC, have been found. ThecreB andcreC mutants grow poorly on some sole carbon sources and have low levels of some enzymes of carbon catabolism e.g. β-galactosidase and D-quinate dehydrogenase. ThecreB andcreC mutants are hypersitive to fluoroacetate, fluoroacetamide and allyl alcohol in the presence of glucose or sucrose but not glycerol; and the enzymes, acetamidase, and alcohol dehydrogenase, are less sensitive to carbon catabolite repression than the wild-type strain. Extracellular protease and α-glucosidase enzyme activities are elevated increB andcreC mutants, while L-proline and L-glutamate uptake capacities are lower in both the presence and absence of glucose. Interactions betweencreA, B and C mutations have been investigated in double mutants, and the dominance properties ofcreB andcreC mutants determined. The results indicate that thecreB andcreC genes may have a regulatory role in the control of carbon catabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00695399
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