3.3.2.2. Proteins detected exclusively in 20% glucose. The 7 spots
detected exclusively in yeast cells during exponential growth in 20%
glucose are listed in Table 3. The locations of the identified proteins
are marked with circles and numbers in the representative gel shown
in Fig. 3c. Some of these proteins are present in multiple forms. We
found the enzyme phosphoglycerate kinase (spot 8) expressed in 20%
glucose; this is a glycolitic/gluconeogenic enzyme. When cells
produce a high amount of ethanol, they use this metabolite as a
carbon source and they convert it into glucose through gluconeogenic
pathway. We also identified 2 spots of the pyruvate decarboxylase 1
enzyme (spots 10 and 11). Pyruvate decarboxylase 1 is the first
enzyme of the fermentation pathway and its expression in cells grown
in 20% glucose agrees with the high rate fermentation that we
evaluated in these cells. Furthermore we saw that the translation
protein elongation factor 2 (spot 13) and the ATP-dependent RNA
helicase (spot 14) which is involved in mitochondrial splicing and also
required for efficient mitochondrial translation, are expressed
exclusively in 20% glucose.
3.3.2.3. Proteins exclusively detected both in 2% glucose and 0.5% glucose.
Among the 7 protein spots, whose expression during the exponential
growth resulted detectable exclusively both in 2% and in 0.5% glucose
(Fig. 3a and b), is the 5-methyltetrahydropteroyl-triglutamatehomocysteine-
methyltransferase which is present in multiple forms.
We identified, in fact, 4 spots (spots 16, 17, 18 and 19) that correspond
to this enzyme which is involved in amino acids metabolism. We also
identified the poly-(A)-binding protein (spot 15), which is part of the
3′-end RNA processing complex and interacts with translation factor
eIF-4G, and the alpha subunit of mitochondrial F1F0 ATP synthase
(spot 21), which is a large, evolutionarily conserved enzyme complex
required for ATP synthesis.3.3.2.4. Proteins exclusively detected both in 2% glucose and 20% glucose.
Of the 18 proteins (Fig. 3a and c) whose expression results inhibited in
0.5% glucose we identified several proteins related to glycolysis and
alcoholic fermentation. Two spots (spots 22 and 23) correspond to the
enzyme pyruvate decarboxylase 1. One spot corresponds to phosphoglycerate
kinase (spot 34), a key enzyme in glycolysis. Two spots
(spots 24 and 25) correspond to fructose 1,6-bisphosphate aldolase,
which is required for glycolysis and 2 spots correspond to enolase 2
(spots 27 and 28) whose expression is glucose-induced. We also
identified 2 spots corresponding to glyceraldehyde-3-phosphate
dehydrogenase 3 (spots 39 and 40). Fig. 5 highlights the major
metabolic pathways affected and the protein spots exclusively
detected in 2% and 20% glucose concentrations.
3.3.2.2. Proteins detected exclusively in 20% glucose. The 7 spotsdetected exclusively in yeast cells during exponential growth in 20%glucose are listed in Table 3. The locations of the identified proteinsare marked with circles and numbers in the representative gel shownin Fig. 3c. Some of these proteins are present in multiple forms. Wefound the enzyme phosphoglycerate kinase (spot 8) expressed in 20%glucose; this is a glycolitic/gluconeogenic enzyme. When cellsproduce a high amount of ethanol, they use this metabolite as acarbon source and they convert it into glucose through gluconeogenicpathway. We also identified 2 spots of the pyruvate decarboxylase 1enzyme (spots 10 and 11). Pyruvate decarboxylase 1 is the firstenzyme of the fermentation pathway and its expression in cells grownin 20% glucose agrees with the high rate fermentation that weevaluated in these cells. Furthermore we saw that the translationprotein elongation factor 2 (spot 13) and the ATP-dependent RNAhelicase (spot 14) which is involved in mitochondrial splicing and alsorequired for efficient mitochondrial translation, are expressedexclusively in 20% glucose.3.3.2.3. Proteins exclusively detected both in 2% glucose and 0.5% glucose.Among the 7 protein spots, whose expression during the exponentialgrowth resulted detectable exclusively both in 2% and in 0.5% glucose(Fig. 3a and b), is the 5-methyltetrahydropteroyl-triglutamatehomocysteine-methyltransferase which is present in multiple forms.We identified, in fact, 4 spots (spots 16, 17, 18 and 19) that correspondto this enzyme which is involved in amino acids metabolism. We alsoidentified the poly-(A)-binding protein (spot 15), which is part of the3′-end RNA processing complex and interacts with translation factoreIF-4G, and the alpha subunit of mitochondrial F1F0 ATP synthase(spot 21), which is a large, evolutionarily conserved enzyme complexrequired for ATP synthesis.3.3.2.4. Proteins exclusively detected both in 2% glucose and 20% glucose.Of the 18 proteins (Fig. 3a and c) whose expression results inhibited in0.5% glucose we identified several proteins related to glycolysis andalcoholic fermentation. Two spots (spots 22 and 23) correspond to theenzyme pyruvate decarboxylase 1. One spot corresponds to phosphoglyceratekinase (spot 34), a key enzyme in glycolysis. Two spots(spots 24 and 25) correspond to fructose 1,6-bisphosphate aldolase,which is required for glycolysis and 2 spots correspond to enolase 2(spots 27 and 28) whose expression is glucose-induced. We alsoidentified 2 spots corresponding to glyceraldehyde-3-phosphatedehydrogenase 3 (spots 39 and 40). Fig. 5 highlights the majormetabolic pathways affected and the protein spots exclusivelydetected in 2% and 20% glucose concentrations.
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3.3.2.2. Proteins detected exclusively in 20% glucose. The 7 spots
detected exclusively in yeast cells during exponential growth in 20%
glucose are listed in Table 3. The locations of the identified proteins
are marked with circles and numbers in the representative gel shown
in Fig. 3c. Some of these proteins are present in multiple forms. We
found the enzyme phosphoglycerate kinase (spot 8) expressed in 20%
glucose; this is a glycolitic/gluconeogenic enzyme. When cells
produce a high amount of ethanol, they use this metabolite as a
carbon source and they convert it into glucose through gluconeogenic
pathway. We also identified 2 spots of the pyruvate decarboxylase 1
enzyme (spots 10 and 11). Pyruvate decarboxylase 1 is the first
enzyme of the fermentation pathway and its expression in cells grown
in 20% glucose agrees with the high rate fermentation that we
evaluated in these cells. Furthermore we saw that the translation
protein elongation factor 2 (spot 13) and the ATP-dependent RNA
helicase (spot 14) which is involved in mitochondrial splicing and also
required for efficient mitochondrial translation, are expressed
exclusively in 20% glucose.
3.3.2.3. Proteins exclusively detected both in 2% glucose and 0.5% glucose.
Among the 7 protein spots, whose expression during the exponential
growth resulted detectable exclusively both in 2% and in 0.5% glucose
(Fig. 3a and b), is the 5-methyltetrahydropteroyl-triglutamatehomocysteine-
methyltransferase which is present in multiple forms.
We identified, in fact, 4 spots (spots 16, 17, 18 and 19) that correspond
to this enzyme which is involved in amino acids metabolism. We also
identified the poly-(A)-binding protein (spot 15), which is part of the
3′-end RNA processing complex and interacts with translation factor
eIF-4G, and the alpha subunit of mitochondrial F1F0 ATP synthase
(spot 21), which is a large, evolutionarily conserved enzyme complex
required for ATP synthesis.3.3.2.4. Proteins exclusively detected both in 2% glucose and 20% glucose.
Of the 18 proteins (Fig. 3a and c) whose expression results inhibited in
0.5% glucose we identified several proteins related to glycolysis and
alcoholic fermentation. Two spots (spots 22 and 23) correspond to the
enzyme pyruvate decarboxylase 1. One spot corresponds to phosphoglycerate
kinase (spot 34), a key enzyme in glycolysis. Two spots
(spots 24 and 25) correspond to fructose 1,6-bisphosphate aldolase,
which is required for glycolysis and 2 spots correspond to enolase 2
(spots 27 and 28) whose expression is glucose-induced. We also
identified 2 spots corresponding to glyceraldehyde-3-phosphate
dehydrogenase 3 (spots 39 and 40). Fig. 5 highlights the major
metabolic pathways affected and the protein spots exclusively
detected in 2% and 20% glucose concentrations.
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