Glucose‐induced inactivation of isocitrate lyase in <i>Saccharomyces cerevisiae</i> is mediated by an internal decapeptide sequence

Ordiz, Isabel; Herrero, Pilar; Rodicio, Rosaura; Moreno, Fernando Salvador

doi:10.1016/0014-5793(95)00538-k

Cited by 20 publications

(13 citation statements)

References 23 publications

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“…Characterisation of this phenomenon has shown that the first step involves reversible inactivation of the enzyme by phosphorylation, while in the second stage final degradation of the protein occurs (Lopez-Boado et al 1988;Ordiz et al 1995). However, preliminary studies of A. nidulans (De Lucas et al 1994b) suggested that proteolysis of the enzyme is the only mechanism involved in the glucose-induced inactivation of isocitrate lyase, although this hypothesis has to be confirmed by additional experiments.…”

Section: Cristina Amor · Ana I Domínguez · J Ramón De Lucas · Fernamentioning

confidence: 88%

The catabolite inactivation of Aspergillus nidulans isocitrate lyase occurs by specific autophagy of peroxisomes

Amor

Domínguez

Lucas

et al. 2000

Archives of Microbiology

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In Aspergillus nidulans, activity of the glyoxylate cycle enzyme isocitrate lyase is finely regulated. Isocitrate lyase is induced by growth on C2 compounds and long-chain fatty acids and repressed by glucose. In addition, activity of isocitrate lyase is subject to a second mechanism of catabolite control, glucose-induced inactivation. Here, we demonstrate that the catabolite inactivation of A. nidulans isocitrate lyase, a process that takes place during glucose adaptation of cells grown under gluconeogenic conditions, occurs by proteolysis of the enzyme. Ultrastructural analyses were carried out in order to investigate the cellular processes that govern the catabolite inactivation of this peroxisomal enzyme. Addition of glucose to oleate-induced cells triggered the specific engulfment and sequestration of peroxisomes by the vacuoles. Sequestration of various peroxisomes by a single vacuole was a frequently observed phenomenon. Results obtained by immunoelectron microscopy using antibodies against A. nidulans isocitrate lyase showed that degradation of this peroxisomal enzyme occurred inside the vacuole. In addition, ultrastructural studies demonstrated that microautophagy was the autophagic pathway involved in degradation of redundant peroxisomes during glucose adaptation of oleate-induced cells of A. nidulans.

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Section: Cristina Amor · Ana I Domínguez · J Ramón De Lucas · Fernamentioning

confidence: 88%

The catabolite inactivation of Aspergillus nidulans isocitrate lyase occurs by specific autophagy of peroxisomes

Amor

Domínguez

Lucas

et al. 2000

Archives of Microbiology

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“…S. cerevisiae FMY402 15 ) (Ordiz et al, 1995), kindly provided by Dr Fernando Moreno (Universidad de Oviedo, Spain), was used in the ICL1 complementation assay.…”

Section: Strains and Culture Conditionsmentioning

confidence: 99%

The ICL1 gene of Pichia pastoris, transcriptional regulation and use of its promoter

Menéndez¹,

Valdés²,

Cabrera³

2003

Yeast

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We cloned and characterized a gene encoding isocitrate lyase from the methylotrophic yeast Pichia pastoris. This gene was isolated from a P. pastoris genomic library using a homologous PCR hybridization probe, amplified with two sets of degenerate primers designed from conserved regions in yeast isocitrate lyases. The cloned gene was sequenced and consists of an open reading frame of 1563 bp encoding a protein of 551 amino acids. The molecular mass of the protein is calculated to be 60.6 kDa with high sequence similarity to isocitrate lyase from other organisms. There is a 64% identity between amino acid sequences of P. pastoris Icl and Saccharomyces cerevisiae Icl. Northern blot analyses showed that, as in S. cerevisiae, the steady-state ICL1 mRNA levels depend on the carbon source used for cell growth. Expression in P. pastoris of the dextranase gene (dexA) from Penicillium minioluteum under control of the ICL1 promoter proved that P ICL1 is a good alternative for the expression of heterologous proteins in this methylotrophic yeast. The sequence presented here has been deposited in the EMBL data library under Accession No. AJ272040.

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“…Determination of galactosidase activities of ICL-␤-galactosidase fusion proteins indicated the importance of a decapeptide sequence, located between amino acid residues 37 and 46 of ICL, for glucose-induced degradation of the enzyme (19). This decapeptide is not present in FBPase and other gluconeogenic enzymes.…”

mentioning

confidence: 99%

Proteins of Newly Isolated Mutants and the Amino-terminal Proline Are Essential for Ubiquitin-Proteasome-catalyzed Catabolite Degradation of Fructose-1,6-bisphosphatase of Saccharomyces cerevisiae

Hämmerle¹,

Bauer²,

Rose³

et al. 1998

Journal of Biological Chemistry

101

131

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Addition of glucose to cells of the yeast Saccharomyces cerevisiae growing on a non-fermentable carbon source leads to selective and rapid degradation of fructose-1,6-bisphosphatase. This so called catabolite inactivation of the enzyme is brought about by the ubiquitin-proteasome system. To identify additional components of the catabolite inactivation machinery, we isolated three mutant strains, gid1, gid2, and gid3, defective in glucose-induced degradation of fructose-1,6-bisphosphatase. All mutant strains show in addition a defect in catabolite inactivation of three other gluconeogenic enzymes: cytosolic malate dehydrogenase, isocitrate lyase, and phosphoenolpyruvate carboxykinase. These findings indicate a common mechanism for the inactivation of all four enzymes. The mutants were also impaired in degradation of short-lived N-end rule substrates, which are degraded via the ubiquitin-proteasome system. Sitedirected mutagenesis of the amino-terminal proline residue yielded fructose-1,6-bisphosphatase forms that were no longer degraded via the ubiquitin-proteasome pathway. All amino termini other than proline made fructose-1,6-bisphosphatase inaccessible to degradation. However, the exchange of the amino-terminal proline had no effect on the phosphorylation of the mutated enzyme. Our findings suggest an essential function of the amino-terminal proline residue for the degradation process of fructose-1,6-bisphosphatase. Phosphorylation of the enzyme was not necessary for degradation to occur.

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Glucose‐induced inactivation of isocitrate lyase in Saccharomyces cerevisiae is mediated by an internal decapeptide sequence

Cited by 20 publications

References 23 publications

The catabolite inactivation of Aspergillus nidulans isocitrate lyase occurs by specific autophagy of peroxisomes

The catabolite inactivation of Aspergillus nidulans isocitrate lyase occurs by specific autophagy of peroxisomes

The ICL1 gene of Pichia pastoris, transcriptional regulation and use of its promoter

Proteins of Newly Isolated Mutants and the Amino-terminal Proline Are Essential for Ubiquitin-Proteasome-catalyzed Catabolite Degradation of Fructose-1,6-bisphosphatase of Saccharomyces cerevisiae

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