Biosynthetic and regulatory role of lys9 mutants of Saccharomyces cerevisiae

Winston, M K; Bhattacharjee, J. K.

doi:10.1007/bf00378182

Cited by 13 publications

(6 citation statements)

References 28 publications

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“…The specific repression by lysine, in particular, results in parallel repression of mRNA and enzyme synthesis, as shown for both LYSl and LYSY genes. This is at variance with the arginine pathway where the specific repression by arginine has been shown to operate at post-transcriptional or even translational levels [21-231. A recent paper [24] reports the derepression of lysine enzymes in Iys9 mutants and proposes that the LYS9 product, in addition to its catalytic function, plays the role of a repressor of the expression of the other LYS genes. This interpretation is, however, difficult to reconcile with the very complete evidence we provide in this work in favour of a regulation involving gene LYS14.…”

Section: Discussionmentioning

confidence: 99%

Control of enzyme synthesis in the lysine biosynthetic pathway of Saccharomyces cerevisiae

Ramos

Dubois

Pierard

1988

European Journal of Biochemistry

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Several enzymes of the lysine pathway of Saccharomyces cerevisiue were found to respond to an induction mechanism mediated by the product of gene LYSl4 in the presence of 2-aminoadipate semialdehyde, an intermediate of this pathway. This novel regulatory mechanism appears independent of the specific repression by lysine and of the general control of amino acid biosynthesis. Genes LYSI, LYS9 and LYSl4 have been cloned and their DNAs used to assay the corresponding messenger RNAs. The results suggest that the induction mechanism, as well as the specific and general regulations, operate at the transcriptional level.The synthesis of saccharopine dehydrogenase (glutamate-forming), previously shown to require the unlinked genes LYS9 and LYS14, is also affected by the induction mechanism. The leaky auxotrophic behaviour of lys14 mutants is explained by the low basal level of expression of LYS9, the structural gene of this enzyme, in the absence of induction by 2-aminoadipate semialdehyde.

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Section: Discussionmentioning

confidence: 99%

Control of enzyme synthesis in the lysine biosynthetic pathway of Saccharomyces cerevisiae

Ramos

Dubois

Pierard

1988

European Journal of Biochemistry

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“…28 The activity is constitutively derepressed in lys9 mutants which are deficient in levels of saccharopine reductase. 29 The relationship of lys9 and lys14 and the role of Lys14 in regulating lysine biosynthesis gene expression is discussed in Section 2.6.…”

Section: Homoisocitrate Dehydrogenasementioning

confidence: 99%

Lysine biosynthesis and metabolism in fungi

Zabriskie¹,

Jackson²

2000

Nat. Prod. Rep.

152

120

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Introduction: lysine biosynthesis 1.1 The a-aminoadipate pathway to l-lysine 2 Enzymes of the a-aminoadipate pathway 2.1 Homocitrate synthase 2.2 Homoaconitate hydratase 2.3 Homoisocitrate dehydrogenase 2.4 a-Aminoadipate aminotransferase 2.5 a-Aminoadipate reductase 2.6 Saccharopine reductase 2.7 Saccharopine dehydrogenase 3 Role of pipecolic acid in lysine biosynthesis 4 Lysine catabolism 5 Role of a-aminoadipate pathway intermediates in secondary metabolism 6 The a-aminoadipate pathway in archaea and bacteria 7 Conclusion 8 Acknowledgements 9 References

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“…Lysine is synthesized in Saccharomyces cerevisiae baker's yeast from ␣-ketoglutarate via ␣-aminoadipate (1) in a linear pathway in which eight enzymatic reactions are involved ( Fig. 1) (10,29,30,34). Some of the enzymes which catalyze the first four steps are located in the mitochondria, whereas the rest are cytosolic (14,15).…”

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Lysine-overproducing mutants of Saccharomyces cerevisiae baker's yeast isolated in continuous culture

Gasent-Ramirez

Benı́tez

1997

Appl Environ Microbiol

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Saccharomyces cerevisiae baker's yeast mutants which produce 3 to 17 times as much lysine as the wild type, depending on the nitrogen source, have been selected. The baker's yeast strain was grown in a pH-regulated chemostat in minimal medium with proline as the nitrogen source, supplemented with increasing concentrations of the toxic analog of the lysine S-2-aminoethyl-L-cysteine (AEC). The lysine-overproducing mutants, which were isolated as AEC-resistant mutants, were also resistant to high external concentrations of lysine and to ␣-aminoadipate and seemed to be affected in the lysine biosynthetic pathway but not in the biosynthetic pathways of other amino acids. Lysine overproduction by one of the mutants seemed to be due to, at least, the loss of repression of the homocitrate synthase encoded by the LYS20 gene. The mutant grew slower than the wild type, and its dough-raising capacity was reduced in in vitro assays, probably due to the toxic effects of lysine accumulation or of an intermediate produced in the pathway. This mutant can be added as a food supplement to enrich the nutritive qualities of bakery products, and its resistance to ␣-aminoadipate, AEC, and lysine can be used as a dominant marker.

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Biosynthetic and regulatory role of lys9 mutants of Saccharomyces cerevisiae

Cited by 13 publications

References 28 publications

Control of enzyme synthesis in the lysine biosynthetic pathway of Saccharomyces cerevisiae

Control of enzyme synthesis in the lysine biosynthetic pathway of Saccharomyces cerevisiae

Lysine biosynthesis and metabolism in fungi

Lysine-overproducing mutants of Saccharomyces cerevisiae baker's yeast isolated in continuous culture

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