A fine-structure map of the yeast L-asparaginase gene

Jones, Gary E.

doi:10.1007/bf00353689

Cited by 14 publications

(7 citation statements)

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“…The characteristics of the two asparaginases indicate that, in this species, the enzymes have evolved to satisfy two different requirements for cellular homeostasis. L-Asparaginase I, which is constitutive and is coded for by a single structural gene (7,10,11), appears to interact primarily with intracellular pools of L-asparagine, perhaps functioning as a part of a mechanism by which these pools are controlled. Asparaginase II, which is derepres-sible by nitrogen starvation and requires tunctional product of at least two genes (3,4,8,9), apparently functions either as a sensor/effector related to the state of nitrogen metabolism in the cell or as an element that responds to a separate sensor of nitrogen balance in the cell.…”

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confidence: 99%

L-Asparagine auxotrophs of Saccharomyces cerevisiae: genetic and phenotypic characterization

Jones¹

1978

J Bacteriol

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L-Asparagine auxotrophy in Saccharomyces cerevisiae is the result of mutation in each of two unlinked cistrons, ASN1 and ASN2. Mutation in only one of these cistrons yields growth indistinguishable from that of wild-type cells under a variety of nutritional stresses. Relatively high concentrations of L-asparagine are required to permit maximal growth of the auxotrophs, and the amino acid requirement cannot be satisfied by a variety of other amino acids that serve as nitrogen sources for cell growth. Although reversion of the mutations can occur, haploid populations of cells containing only low frequencies of prototrophs can be maintained easily. In diploid cells heteroallelic for certain combinations of alleles of the two genes, mitotic recombination gives rise to prototrophic cells that accumulate to high frequency in populations of the cells.

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confidence: 99%

L-Asparagine auxotrophs of Saccharomyces cerevisiae: genetic and phenotypic characterization

Jones¹

1978

J Bacteriol

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“…They suggested that a single yeast L-asparaginase existed which was synthe-sized constitutively, was entirely intracellular in nature, and was functionally unaffected by the products of its activity. Concurrently, they investigated the genetic control of L-asparaginase synthesis and through the aid of asparaginaseless mutants were able to show a single structural gene (called aspl) was responsible for asparaginase synthesis (7,8).…”

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confidence: 99%

L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme

Dunlop

Roon²

1975

J Bacteriol

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During recent studies conducted with suspensions of three strains of Saccharomyces cerevisiae, it was observed that ammonia was rapidly liberated when L-asparagine was added to the medium. Subsequent investigation has revealed that these strains of S. cerevisiae have an extemally active asparaginase as well as an internally active one. The appearance of the external asparaginase is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The internal enzyme appears to be constitutive. The external activity is relatively insensitive to para-hydroxymercuribenzoate inhibtion, whereas the internal activity is highly inhibited by this compound.

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“…ASP1 and ASP3 encode for the enzymes cytosolic l ‐asparaginase and cell wall l ‐asparaginase II, respectively, which hydrolyze l ‐asparagine as well as, in the case of ASP3 , d ‐asparagine to aspartate and ammonia (Dunlop et al ., ). Whereas ASP1 is constitutively expressed in the cell, ASP3 is upregulated during nitrogen starvation to facilitate the utilization of extracellular asparagine as a source of nitrogen (Jones, ; Jones & Mortimer, ; Dunlop & Roon, ).…”

Section: Asp3 Polymorphism Within Saccharomyces Cerevisiae Strainsmentioning

confidence: 99%

TheASP3locus inSaccharomyces cerevisiaeoriginated by horizontal gene transfer fromWickerhamomyces

2012

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The asparagine degradation pathway in the S288c laboratory strain of Saccharomyces cerevisiae is comprised of genes located at two separate loci. ASP1 is located on chromosome IV and encodes for cytosolic l‐asparaginase I, whereas ASP3 contains a gene cluster located on chromosome XII comprised of four identical genes, ASP3‐1, ASP3‐2, ASP3‐3, and ASP3‐4, which encode for cell wall‐associated l‐asparaginase II. Interestingly, the ASP3 locus appears to be only present, in variable copy number, in S. cerevisiae strains isolated from laboratory or industrial environments and is completely absent from the genomes of 128 diverse fungal species. Investigation of the evolutionary history of ASP3 across these 128 genomes as well as across the genomes of 43 S. cerevisiae strains shows that ASP3 likely arose in a S. cerevisiae strain via horizontal gene transfer (HGT) from, or a close relative of, the wine yeast Wickerhamomyces anomalus, which co‐occurs with S. cerevisiae in several biotechnological processes. Thus, because the ASP3 present in the S288c laboratory strain of S. cerevisiae is induced in response to nitrogen starvation, its acquisition may have aided yeast adaptation to artificial environments. Our finding that the ASP3 locus in S. cerevisiae originated via HGT further highlights the importance of gene sharing between yeasts in the evolution of their remarkable metabolic diversity.

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A fine-structure map of the yeast L-asparaginase gene

Cited by 14 publications

References 10 publications

L-Asparagine auxotrophs of Saccharomyces cerevisiae: genetic and phenotypic characterization

L-Asparagine auxotrophs of Saccharomyces cerevisiae: genetic and phenotypic characterization

L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme

TheASP3locus inSaccharomyces cerevisiaeoriginated by horizontal gene transfer fromWickerhamomyces

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