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  • 1
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The identification, isolation and characterization of a new Aspergillus nidulans positive-acting gene metR, which encodes a transcriptional activator of sulphur metabolism, is reported. metR mutants are tight auxotrophs requiring methionine or homocysteine for growth. Mutations in the metR gene are epistatic to mutations in the negative-acting sulphur regulatory scon genes. The metR coding sequence is interrupted by a single intron of 492 bp which is unusually long for fungi. Aspergillus nidulans METR is a member of bZIP family of DNA-binding proteins. The bZIP domains of METR and the Neurospora crassa CYS3 transcriptional activator of sulphur genes are highly similar. Although Neurospora cys-3 gene does not substitute for the metR function, a chimeric metR gene with a cys-3 bZIP domain is able to transform the ΔmetR mutant to methionine prototrophy. This indicates that METR recognizes the same regulatory sequence as CYS3. The metR gene is not essential, as deletion mutants are viable and have similar phenotype as point mutants. In contrast to the Neurospora cys-3, transcription of the metR gene was found to be regulated neither by METR protein nor by sulphur source. Transcription of metR gene is derepressed in the sconB2 mutant. Transcription of genes encoding sulphate permease, homocysteine synthase, cysteine synthase, ATP-sulphurylase, and sulphur controller –sconB is strongly regulated by the metR gene product and depends on the character of the metR mutation and sulphur supplementation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 259 (1976), S. 337-338 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sulphate permease in A. nidulans is completely repressed if the mycelium is grown in the presence of cysteine, homocysteine or methionine. Toxicity of chrornate, a substrate to the sulphate permease, is therefore easily reversed by the addition of methionine to the growth medium. More than 100 ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 204 (1964), S. 809-809 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] There are at least three possible explanations of the 'selfers' phenomenon : (a) unequal crossing-over; (6) copy-choice (non -reciprocal exchange) connected with illegitimate conjugation of similar components of structures involved in recombination; and (c) stimulation of mutability of the locus by ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The fission yeast Schizosaccharomyces pombe has a unique organization of sulfur amino acid metabolism: it has two distinct O-acetylhomoserine sulfhydrylases (homocysteine synthases). Similar to Enterobacteriaceae, S. pombe lacks cystathionine β-synthase and cystathionine γ-lyase - the enzymes of the reverse transsulfuration pathway, by which methionine is readily metabolized to cysteine - a likely effector in the sulfur metabolite repression system. Consequently no repression of sulfate assimilation is observed when methionine is added to the growth medium.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 35 (1999), S. 638-646 
    ISSN: 1432-0983
    Keywords: Key wordsAspergillus nidulans ; Cystathionine β-lyase ; [EC 4.4.1.8] ; metG gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The metG gene of Aspergillus nidulans encoding cystathionine β-lyase, an enzyme of the main pathway of methionine synthesis, was cloned by complementation of a metG mutation. A comparison of metG genomic DNA and a cDNA copy derived from different A. nidulans strains revealed a marked DNA sequence polymorphism manifested mostly by silent point mutations. cDNA of the A. nidulans metG gene complemented the Escherichia coli metC69 mutation impairing cystathionine β-lyase. This gene contains two introns and codes for a protein of 439 amino acids. The protein shows homology with bacterial, yeast and plant cystathionine β-lyases, as well as with other enzymes belonging to a large family of pyridoxal 5′-phosphate binding proteins. Transcription of the metG gene is not appreciably regulated by the concentration of sulphur source in the growth medium.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0983
    Keywords: S. cerevisiae ; Sulphur amino acids ; Regulatory effectors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary cys4-1, a mutation in the reverse trans-sulphuration pathway, relieves the sulphate assimilation pathway and homocysteine synthase from methionine-mediated repression. Since the mutation blocks the synthesis of cysteine from methionine downstream from homocysteine, this indicates that neither methionine nor S-adenosylmethionine serve as low-molecular-mass effectors in this regulatory system, contradicting earlier hypotheses.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 132 (1974), S. 307-320 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary It was found that in Aspergillus nidulans the enzymes of the sulfate assimilation pathway and O-acetylhomoserine sulfhydrylase are under cysteine- and/or homocysteine, but not methionine- or S-adenosylmethionine-mediated regulation. These enzymes are repressed when the cells are grown in the presence of cysteine or homocysteine even in conditions where cysteine cannot be a precursor of homocysteine and vice versa. This was demonstrated by using mutants with impaired cystathionine cleavage enzymes. Thus, these two amino acids can substitute each other as the regulatory effectors. The addition of methionine causes repression only in conditions when it can be metabolized to homocysteine. The mutant cysA1 with a block at the serine transacetylase step is a prototroph owing to the existence of an alternative pathway for cysteine synthesis involving the enzymes: homocysteine synthase, cystathionine β-synthase and γ-cystathionase. All the three enzymes as well as those of the sulfate assimilation pathway are derepressed in this mutant. CysA1 mutation supresses the meth55 mutant blocked at β-cystathionase owing to the derepression of homocysteine synthase, so that the cystathionine cleavage step is bypassed. The results indicate that the pathway involving cystathionine formation is the main one for methionine biosynthesis in A. nidulans. The pathway involving homocysteine synthase is an alternative-conditional one, physiologically effective only when this enzyme is derepressed.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 174 (1979), S. 33-38 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary ATP-sulfurylase, cysteine synthase, homocysteine synthase, arylsulfatase and β-cystathionase in Saccharomycopsis lipolytica are repressed on the addition of methionine, homocysteine or cysteine to the growth medium. The use of appropriate mutants enabled us to demonstrate that the synthesis of these enzymes is regulated by the system involving at least two low-molecular weight effectors — most likely cysteine and methionine (or their close derivatives).
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 186 (1982), S. 355-363 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Genetic studies suggest that the so-called “phosphorus-family of enzymes inN. crassa are controlled by a complex system of regulatory genes which are responsive to the level of phosphorus in the growth medium. The intracellular metabolite(s) that interact with this system to signal changes in the external phosphorus concentration has not been identified. In this study the pools of acid-soluble, phosphorus-containing, compounds are measured in wild-type and “phosphorus-family” enzyme regulatory mutant strains ofN. crassa before and during phosphorus starvation. Prolonged phosphorus starvation of wild-typeN. crassa failed to alter significantly the pre-starvation level of intracellular orthophosphate, suggesting that intracellular Pi would be a poor effector signal for the control of the phosphorus family enzymes. However, inorganic pyrophosphate (PPi) decreased 15-fold, and tri- and tetrapolyphosphate (PPPi and PPPPi) increased 3- to 5-fold within 15 minutes after transfer of the wild-type strain to phosphorus-free medium. Phosphate starvation of seven different regulatory gene mutant strains resulted in a rapid decrease in the PPi pool similar to that which occurred in the wild-type. However, only two of these seven strains showed increased PPPi and PPPPi pools following phosphate starvation. Additional experiments demonstrated that PPi pools, but not PPPi and PPPPi pools, were unaffected by several starvation regimens other than phosphorus starvation. Metabolic studies employing H3 32PO4 showed that the pool of PPi was labeled to steady-state levels after two minutes of continuous labeling of a phosphate-sufficient culture. Furthermore, long-term steady-state labeling showed that the intracellular PPi pool was directly responsive to the decrease in the extracellular Pi concentration of the medium resulting from cell growth. Growth on phosphoethanolamine, a phosphorus source that allows a modest degree of derepression even in growing cells, resulted in lower levels of PPi than were seen in phosphate-grown cells. These observations suggest that PPi may be involved in the mechanism responsible for the control of phosphorus-family enzyme regulatory gene product activity.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 155 (1977), S. 109-112 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants of Aspergillus nidulans blocked in the main pathway of cysteine synthesis show an elevated level of the enzymes involved in the synthesis of cysteine from homocysteine i.e. cystathionine β-synthase and γ-cystathionase and a depressed level of homocysteine methyltransferase. This results in a considerable change in the sulfur amino acids pool as compared to the wild type. Upon addition of cysteine to the growth medium the first two enzymes are repressed while the level of the third one increases. These data indicate that the two diverging pathways of homocysteine metabolism are anti-coordinately regulated.
    Type of Medium: Electronic Resource
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