Catabolism of bis(5'-nucleosidyl) tetraphosphates in Saccharomyces cerevisiae

Plateau, Pierre; Fromant, Michel; Schmitter, Jean‐Marie; Blanquet, Sylvain

doi:10.1128/jb.172.12.6892-6899.1990

Cited by 42 publications

(44 citation statements)

References 33 publications

(28 reference statements)

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“…Figure 3 shows that the transcript levels of all three genes increase significantly in amount within 2-30 min after the shift and continue to increase steadily up to 90 min. As in S. cerevisiae, expression of the KlAPA2 and KIFPS1 genes is only slightly affected by the change of carbon source (Anderson et al 1989;Plateau et al 1990). Fig.…”

Section: Glucose Fails To Affect the Level Of Expression Of K Lactismentioning

confidence: 99%

Carbon catabolite regulation of transcription of nuclear genes coding for mitochondrial proteins in the yeast Kluyveromyces lactis

1995

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Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Carbon catabolite regulation of transcription of nuclear genes coding for mitochondrial proteins in the yeast Kluyveromyces lactis Received: 7 February 1995 Abstract Promoter regions of the K1QCR7, KlQCR8 and K1CYC1 genes, coding for subunits of the bclcomplex and cytochrome c respectively, in the shortterm Crabtree-negative yeast Kluyveromyces Iactis differ markedly in sequence from their Saccharomyces cerevisiae counterparts. They have, however, conserved very similar configurations of binding-site motifs for various transcription factors known to be involved in global and carbon-source regulation in S. cerevisiae. To investigate the carbon source-dependent expression of these genes in K. lactis, we have carried out mediumshift experiments and determined transcript levels during the shifts. In sharp contrast to the situation in S. cerevisiae, the level of expression in K. lactis is not affected when glucose is added to a non-fermentable carbon-source medium. However, the genes are not constitutively expressed, but become significantly induced when the cells are shifted from glucose to a nonfermentable carbon source. Finally, induction of transcriptional activation does not occur in media containing both glucose and non-fermentable carbon sources.

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Section: Glucose Fails To Affect the Level Of Expression Of K Lactismentioning

confidence: 99%

Carbon catabolite regulation of transcription of nuclear genes coding for mitochondrial proteins in the yeast Kluyveromyces lactis

1995

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“…Various bis(5'-nucleosidyl) polyphosphates, e.g., Ap4N (N = A, C, G, or U) (13,40), Ap3N (5,9,12,19,25,27,28), Bp4B' (B, B' = C, G, or U) (8,10), Gp3G (35,39), and Ap5A (32), occur in living cells. These nucleotides are believed to have a physiological role because their intracellular concentrations may depend on environmental factors such as temperature or the presence of oxidants.…”

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Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae

Brevet¹,

Chen²,

Fromant³

et al. 1991

J Bacteriol

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An enzyme able to cleave dinucleoside triphosphates has been purified 3,750-fold from Saccharomyces cerevisiae. Contrary to the enzymes previously shown to catabolize Ap4A in yeast, this enzyme is a hydrolase rather than a phosphorylase. The dinucleoside triphosphatase molecular ratio estimated by gel filtration is 55,000. Dinucleoside triphosphatase activity is strongly stimulated by the presence of divalent cations. Mn2+ displays the strongest stimulating effect, followed by Mg2+, Co2+, Cd2+, and Ca2+. The Km value for Ap3A is 5.4 microM (50 mM Tris-HCl [pH 7.8], 5 mM MgCl2, and 0.1 mM EDTA; 37 degrees C). Dinucleoside polyphosphates are substrates of this enzyme, provided that they contain more than two phosphates and that at least one of the two bases is a purine (Ap3A, Ap3G, Ap3C, Gp3G, Gp3C, m7Gp3A, m7Gp3G, Ap4A, Ap4G, Ap4C, Ap4U, Gp4G, and Ap5A are substrates; AMP, ADP, ATP, Ap2A, and Cp4U are not). Among the products, a nucleoside monophosphate is always formed. The specificity of cleavage of methylated dinucleoside triphosphates and the molecular weight of dinucleoside triphosphatase indicate that this enzyme is different from the mRNA decapping enzyme previously characterized (A. Stevens, Mol. Cell. Biol. 8:2005-2010, 1988).

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“…In Saccharomyces cerevisiae, Ap4A is degraded by two similar phosphorylases (29,30). Phosphorolysis of Ap4A in the presence of Pi and a divalent cation yields ADP and ATP (18).…”

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“…Phosphorolysis of Ap4A in the presence of Pi and a divalent cation yields ADP and ATP (18). About 80 to 85% of the endogenous Ap4A is catabolized by Ap4A phosphorylase 1 (29,30). The APAI gene encoding this enzyme has been cloned and sequenced (22,30) and physically mapped on chromosome III (16,22).…”

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A paradoxical increase of a metabolite upon increased expression of its catabolic enzyme: the case of diadenosine tetraphosphate (Ap4A) and Ap4A phosphorylase I in Saccharomyces cerevisiae

et al. 1991

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The APA1 gene in Saccharomyces cerevisiae encodes Ap4A phosphorylase I, the catabolic enzyme for diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A). APA1 has been inserted into a multicopy plasmid and into a centromeric plasmid with a GAL1 promoter. Enhanced expression of APA1 via the plasmids resulted in 10- and 90-fold increases in Ap4A phosphorylase activity, respectively, as assayed in vitro. However, the intracellular concentration of Ap4A exhibited increases of 2- and 15-fold, respectively, from the two different plasmids. Intracellular Ap4A increased 3- to 20-fold during growth on galactose of a transformant with APA1 under the control of the GAL1 promoter. Intracellular adenosine 5'-P1-tetraphospho-P4-5"'-guanosine (Ap4G) and diguanosine 5',5"'-P1,P4-tetraphosphate (Gp4G) also increased in the transformant under these conditions. The chromosomal locus of APA1 has been disrupted in a haploid strain. The Ap4A phosphorylase activity decreased by 80% and the intracellular Ap4A concentration increased by a factor of five in the null mutant. These results with the null mutant agree with previous results reported by Plateau et al. (P. Plateau, M. Fromant, J.-M. Schmitter, J.-M. Buhler, and S. Blancquet, J. Bacteriol. 171:6437-6445, 1989). The paradoxical increase in Ap4A upon enhanced expression of APA1 indicates that the metabolic consequences of altered gene expression may be more complex than indicated solely by assay of enzymatic activity of the gene product.

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Catabolism of bis(5'-nucleosidyl) tetraphosphates in Saccharomyces cerevisiae

Cited by 42 publications

References 33 publications

Carbon catabolite regulation of transcription of nuclear genes coding for mitochondrial proteins in the yeast Kluyveromyces lactis

Carbon catabolite regulation of transcription of nuclear genes coding for mitochondrial proteins in the yeast Kluyveromyces lactis

Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae

A paradoxical increase of a metabolite upon increased expression of its catabolic enzyme: the case of diadenosine tetraphosphate (Ap4A) and Ap4A phosphorylase I in Saccharomyces cerevisiae

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