Proline biosynthesis in Saccharomyces cerevisiae: analysis of the PRO3 gene, which encodes delta 1-pyrroline-5-carboxylate reductase

Brandriss, M C; Falvey, Darlene

doi:10.1128/jb.174.15.5176b.1992

Cited by 23 publications

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“…Whether the PRO homologous sequences mediate any specific regulation remains to be determined, although in this study, expression of the PROJ gene in wild-type yeast strains was not reduced by the addition of proline to the growth medium. The PRO3 gene encoding P5C reductase, the last enzyme in the proline biosynthetic pathway, is also not repressed by the presence of proline in the growth medium (13).…”

Section: Discussionmentioning

confidence: 99%

“…The -y-glutamyl kinase activity was undetectable unless the purified -y-glutamyl phosphate reductase was added to the in vitro assay system (55 (13).…”

Section: Discussionmentioning

confidence: 99%

“…The yeast Saccharomyces cerevisiae synthesizes proline from glutamate via the intermediates y-glutamyl phosphate, -y-glutamyl semialdehyde, and A1-pyrroline-5-carboxylic acid (P5C) (12,13,49,59). The same pathway is found in members of the family Enterobactenaceae (for a review, see reference 38) and mammals (56,60).…”

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confidence: 93%

“…The gene-enzyme relationships were demonstrated by interspecies complementation of proB, proA, and proC mutants of Escherichia coli and Salmonella typhimurium by the yeast PRO], PRO2, and PRO3 genes, respectively (59), and of a yeast prol mutant by the E. coli proB gene (49). There is substantial deduced amino acid sequence similarity between the E. coli (23) and S. cerevisiae (this work) -y-glutamyl kinases, between the E. coli (23) and S. cerevisiae (10) -y-glutamyl phosphate reductases, and among the P5C reductases of bacteria (24,30,52), S. cerevisiae (13), plants (22), and mammals (27).…”

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Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase

Brandriss

1992

J Bacteriol

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The PROJ gene of Saccharomyces cerevisiae encodes the 428-amino-acid protein y-glutamyl kinase (ATP:L-glutamate 5-phosphotransferase, EC 2.7.2.11), which catalyzes the first step in proline biosynthesis. Amino acid sequence comparison revealed significant homology between the yeast and Escherichia coli -y-glutamyl kinases throughout their lengths. Four close matches to the consensus sequence for GCN4 protein binding and one close match to the RAP1 protein-binding site were found in the PROJ upstream region. The response of the PROJ gene to changes in the growth medium was analyzed by measurement of steady-state mRNA levels and of 13-galactosidase activity encoded by a PROJ-lacZ gene fusion. PROJ expression was not repressed by exogenous proline and was not induced by the presence of glutamate in the growth medium. Although expression of the PROJ gene did not change in response to histidine starvation, both steady-state PROJ mRNA levels and 13-galactosidase activities were elevated in a gcdJ strain and reduced in a gcn4 strain.In addition, a pro) bradytrophic strain became completely auxotrophic for proline in a gcn4 strain background. These results indicate that PROJ is regulated by the general amino acid control system.The yeast Saccharomyces cerevisiae synthesizes proline from glutamate via the intermediates y-glutamyl phosphate, -y-glutamyl semialdehyde, and A1-pyrroline-5-carboxylic acid (P5C) (12,13,49,59). The same pathway is found in members of the family Enterobactenaceae (for a review, see reference 38) and mammals (56, 60). The three enzymes involved in this pathway are -y-glutamyl kinase (the product of the PROI gene), -y-glutamyl phosphate reductase (the product of the PRO2 gene), and P5C reductase (the product of the PRO3 gene). The gene-enzyme relationships were demonstrated by interspecies complementation of proB, proA, and proC mutants of Escherichia coli and Salmonella typhimurium by the yeast PRO], PRO2, and PRO3 genes, respectively (59), and of a yeast prol mutant by the E. coli proB gene (49). There is substantial deduced amino acid sequence similarity between the E. coli (23) and S. cerevisiae (this work) -y-glutamyl kinases, between the E. coli (23) and S. cerevisiae (10) -y-glutamyl phosphate reductases, and among the P5C reductases of bacteria (24, 30, 52), S. cerevisiae (13), plants (22), and mammals (27).Proline-requiring S. cerevisiae strains were isolated long after auxotrophs for almost all of the other amino acids had been obtained (12). This was because of their peculiar property of being unable to grow in the standard rich medium in common use in yeast laboratories. Repression and inactivation of both the general amino acid and the proline-specific permeases in media rich in nitrogen sources (20) is believed to be responsible for this inability of proline auxotrophs to grow.

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Section: Discussionmentioning

confidence: 99%

“…The -y-glutamyl kinase activity was undetectable unless the purified -y-glutamyl phosphate reductase was added to the in vitro assay system (55 (13).…”

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 93%

mentioning

confidence: 99%

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Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase

Brandriss

1992

J Bacteriol

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“…This pathway for proline biosynthesis has been established in Escherichia coli, Bacilltls spp. and other bacterial species (Baumberg & Klingel, 1993;Hayzer & Leisinger, 1981 ;Leisinger, 1987), as well as the yeast Saccharomyes cerevisiae (Brandriss & Falvey, 1992).…”

Section: Introductionmentioning

confidence: 99%

Proline is biosynthesized from arginine in Staphylococcus aureus

et al. 1996

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Staphylococcus aureus NCTC 8325 exhibited a long lag phase (11 h) when inoculated into defined medium lacking proline, that could be shortened by increasing the concentration of arginine in the medium, or by supplying ornithine. Radioactivity from ~-['~C]arginine, but not ~-[l~C]glutamate was incorporated into a spot with the chromatographic mobility of [14C]proline in the pool metabolites fraction. Selection for transposon TnSI7-lacZ mutants impaired in arginine catabolism yielded four proline auxotrophs. Enzyme assays and precursor feeding experiments suggested that the major pathway for proline biosynthesis in S. aureus was from arginine via ornithine and A'-pyrroline 5-carboxylate, rather than from glutamate. Strain 8325 Pro+, a proline prototrophic variant obtained by cultivation of 8325 in the absence of proline, accumulated ~-[l~C]arginine from the medium at about eight times the rate of strain 8325, suggesting its response to proline starvation was to increase arginine uptake.1

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The proline biosynthesis in living organisms

Aral

Kamoun

1997

Amino Acids

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Summary.In this article we review recent work on the physiology of proline and Al-pyrroline-5-carboxylate (P5C) in living organisms and consider recent progress in our understanding of the role of P5C synthetase in collagen metabolism and the regulation of urea cycle in vertebrates. Much of this recent progress has been made possible by advances in our knowledge of the enzymes and genes involved in proline biosynthesis in man. The availability of well characterized P5C synthetase deficiency in man has been an impetus for the cloning of the cDNA encoding for this enzyme from man and facilitated the establishment of the phenotype-genotype relationships in PSC synthetase deficiency in higher vertebrates.

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Proline biosynthesis in Saccharomyces cerevisiae: analysis of the PRO3 gene, which encodes delta 1-pyrroline-5-carboxylate reductase

Cited by 23 publications

References 0 publications

Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase

Proline biosynthesis in Saccharomyces cerevisiae: molecular analysis of the PRO1 gene, which encodes gamma-glutamyl kinase

Proline is biosynthesized from arginine in Staphylococcus aureus

The proline biosynthesis in living organisms

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