[76] β-d-Fructofuranoside fructohydrolase from yeast

Goldstein, Alan H.; Lampen, J. O.

doi:10.1016/0076-6879(75)42159-0

Cited by 456 publications

(234 citation statements)

References 7 publications

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“…Cell lysate preparation was performed as described previously . The invertase enzyme assay was done as described previously (Goldstein and Lampen, 1975), with minor modifications: We used M glucose/min/OD 600 for the unit of invertase activity, instead of using M glucose/min/mg.…”

Section: Invertase Assaymentioning

confidence: 99%

Atg27 Is Required for Autophagy-dependent Cycling of Atg9

Yen

Legakis

Nair

et al. 2007

MBoC

162

142

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Autophagy is a catabolic pathway for the degradation of cytosolic proteins or organelles and is conserved among all eukaryotic cells. The hallmark of autophagy is the formation of double-membrane cytosolic vesicles, termed autophagosomes, which sequester cytoplasm; however, the mechanism of vesicle formation and the membrane source remain unclear. In the yeast Saccharomyces cerevisiae, selective autophagy mediates the delivery of specific cargos to the vacuole, the analog of the mammalian lysosome. The transmembrane protein Atg9 cycles between the mitochondria and the pre-autophagosomal structure, which is the site of autophagosome biogenesis. Atg9 is thought to mediate the delivery of membrane to the forming autophagosome. Here, we characterize a second transmembrane protein Atg27 that is required for specific autophagy in yeast. Atg27 is required for Atg9 cycling and shuttles between the pre-autophagosomal structure, mitochondria, and the Golgi complex. These data support a hypothesis that multiple membrane sources supply the lipids needed for autophagosome formation.

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Section: Invertase Assaymentioning

confidence: 99%

Atg27 Is Required for Autophagy-dependent Cycling of Atg9

Yen

Legakis

Nair

et al. 2007

MBoC

162

142

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“…Samples were then removed at the indicated time points, and cells were metabolically poisoned by the addition of 10 mM NaN 3 . Invertase activity of equal number of cells was determined as described by Goldstein and Lampen (1975). Gas1p and carboxypeptidase Y (CPY) maturation was analyzed as described by Munn et al (1999), and Kar2p secretion was monitored as described by ElrodErickson and Kaiser (1996).…”

Section: Protein Maturation and Secretion Assaysmentioning

confidence: 99%

Lipid-dependent Subcellular Relocalization of the Acyl Chain Desaturase in Yeast

Tatzer¹,

Zellnig

Kohlwein

et al. 2002

MBoC

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The degree of acyl chain desaturation of membrane lipids is a critical determinant of membrane fluidity. Temperature-sensitive mutants of the single essential acyl chain desaturase, Ole1p, of yeast have previously been isolated in screens for mitochondrial inheritance mutants (Stewart, L.C., and Yaffe, M.P. ). J. Cell Biol. 115, 1249 -1257. We now report that the mutant desaturase relocalizes from its uniform ER distribution to a more punctuate localization at the cell periphery upon inactivation of the enzyme. This relocalization takes place within minutes at nonpermissive conditions, a time scale at which mitochondrial morphology and inheritance is not yet affected. Relocalization of the desaturase is fully reversible and does not affect the steady state localization of other ER resident proteins or the kinetic and fidelity of the secretory pathway, indicating a high degree of selectivity for the desaturase. Relocalization of the desaturase is energy independent but is lipid dependent because it is rescued by supplementation with unsaturated fatty acids. Relocalization of the desaturase is also observed in cells treated with inhibitors of the enzyme, indicating that it is independent of temperature-induced alterations of the enzyme. In the absence of desaturase function, lipid synthesis continues, resulting in the generation of lipids with saturated acyl chains. A model is discussed in which the accumulation of saturated lipids in a microdomain around the desaturase could induce the observed segregation and relocalization of the enzyme.

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“…Samples were taken at 30-min intervals. Invertase activity was measured according to [27] using whole cells from the mid-exponential phase. Protein was determined with the Biorad protein assay kit using bovine serum albumin as a standard.…”

Section: Assays For Metabolites Enzyme and Glucose Uptakementioning

confidence: 99%

Glucose Uptake and Metabolism in grr1/cat80 Mutants of Sacharomyces cerevisiae

Özcan

Schulte

Freidel

et al. 1994

European Journal of Biochemistry

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Glucose repression in the yeast Saccharomyces cerevisiae designates a global regulatory system controlling the expression of various sets of genes required for the utilization of alternate carbon sources. In a screen, designed for the selection of mutants with reduced glycolytic flux we obtained isolates which were shown by complementation of the cloned wild-type gene to be allelic to the glucose repression mutants grrllcat80lcot2 previously described. We demonstrate that the grrl lesion lead to a concentration-dependent decrease in glycolytic flux on glucose. It is very likely that this is caused by a significant decrease in the expression of various genes encoding hexose transporters (HXTI,3) leading to a reduced glucose-uptake rate. In contrast, expression of the maltose permease gene (MALll) and maltose utilization is normal. There is indirect evidence that grrl affects the uptake of amino acids, and others have shown that the sugar-induced transport of divalent cations is impaired. These effects are not glucose-specific. We suggest that Grrl, a putative cytoplasmic protein, has a central function in the sensing of nutritional conditions for a variety of unrelated substances, and that relief from glucose repression may be a corollary of this defect in sensing.In the yeast Saccharomyces cerevisiae glucose or other readily fermentable carbon sources act as global regulators of growth and metabolism. These regulatory effects are executed partly at the transcriptional level. Glucose repression and glucose induction designate mechanisms that exert specific control on glucose-sensitive genes. Glucose-repressible genes include SUC2 (invertase) and genes that are required for the utilization of alternate carbohydrates (the GAL, MAL and MEL regulons required for the utilization of galactose, maltose and melibiose, respectively; for review see [l]), mitochondrial genes [2] and nuclear genes for mitochondrial and gluconeogenic functions [3]. Analysis of glucose induction at the gene expression level is less advanced. Nevertheless, glucose or its metabolism exerts a plethora of activating effects on many cellular functions. It is not clear, in which way glucose repression and induction are functionally linked.Glucose repression mechanisms in S. cerevisiae have been revealed by means of appropriate mutants either defective in repression or in derepression (for review, see [4]). Analysis of individual mutants allowed in some cases the identification or localization of the regulatory defect. A number of such mutants lead to the identification of transcription factors or transcriptional regulators of glucose-sensitive genes. There are a number of mutants which apparently affect functions early in the signalling pathway for glucoseCorrespondence to

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[76] β-d-Fructofuranoside fructohydrolase from yeast

Cited by 456 publications

References 7 publications

Atg27 Is Required for Autophagy-dependent Cycling of Atg9

Atg27 Is Required for Autophagy-dependent Cycling of Atg9

Lipid-dependent Subcellular Relocalization of the Acyl Chain Desaturase in Yeast

Glucose Uptake and Metabolism in grr1/cat80 Mutants of Sacharomyces cerevisiae

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