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PubMed1988

Substrate specificity of the phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae.

Enzymatic dephosphorylation of the phosphorylated forms of five different yeast enzymes has been studied: fructose-1,6-bisphosphatase, glycogen phosphorylase, neutral trehalase, NAD-glutamate dehydrogenase and 6-phosphofructo-2-kinase. Phosphorylated fructose-1,6-bisphosphatase and phosphorylated 6-phosphofructo-2-kinase were present in extracts of starved yeast cells which had been incubated for 10 min with glucose. Phosphorylated glycogen phosphorylase, neutral trehalase and NAD-glutamate dehydrogenase were obtained by incubation of yeast extract with ATP, cyclic AMP and Mg2+. After incubation with commercially available preparations of alkaline phosphatase, all five phosphorylated enzymes studied showed the changes in catalytic activity that would be expected as a consequence of dephosphorylation. The recently purified yeast enzyme which dephosphorylates phosphorylated fructose-1,6-bisophosphatase (Horn and Holzer (1987) however, was found to be active only with the phosphorylated fructose-1,6-bisphosphatase, but not with the other four phosphorylated enzymes studied. By contrast, a crude extract from yeast showed dephosphorylating activity towards all five substrates. Substrate specificity with the five phosphorylated enzymes studied of different phosphoprotein phosphatases from yeast prepared by others is discussed.

Fructose-Bisphosphatase↗
PubMed1989

Ethanol inhibition of Saccharomyces and Candida enzymes.

Ethanol inhibition of several hydrolases (sucrase, maltase, trehalase, melezitase and cellobiase) has been measured in both highly ethanol-tolerant Saccharomyces strains (R) and in Candida strains less tolerant to ethanol (S). Cells were either grown in the presence of ethanol and the activities of the enzymes measured without preincubation in this alcohol ("in situ" inhibition assay), or the culture was grown in the absence of ethanol and the activities of the enzymes were determined after preincubation and in the presence of this compound ("in vitro" inhibition assay). Ethanol inhibition (Ki values) of sucrase, maltase, trehalase, and melezitase was quite different for these different enzymes in the same strain (R or S), but similar for the same enzyme in different strains (R and S). The Ki values for cellobiase, which is absent from the R strain, were higher when induced than at the basal level and higher in in vitro assays than in in situ assays. This suggests that the inhibition observed in situ is mainly the result of an inhibition of other proteins related to cellobiase (i.e., those involved in its synthesis) but not a direct inactivation of the enzyme by ethanol. Accordingly, when hybrids between Saccharomyces (R) and Candida (S) strains were constructed by protoplast fusion, and cellobiase was measured in the parental Candida strain and some of the hybrids, there was an increase in the Ki values in the in situ assays from 2.25% ethanol in Candida to 5.5% in some of the hybrids.

Candida↗
PubMed1992

Protein synthesis during germination of heterothallic yeast ascospores.

Protein synthesis during ascospore germination of the heterothallic Saccharomyces cerevisiae strain AP-3 was investigated. Protein synthesis in the germinating ascospores appeared to begin approximately 20 min following glucose initiation. Since RNA synthesis did not start until approximately 70 min after the onset of germination, strain AP-3 ascospores must contain RNA which is ready for immediate translation. Both trehalase and glyceraldehyde-3-phosphate dehydrogenase activities were found to be affected by the onset of germination. Trehalase activity was found to increase severalfold following 60 min of spore germination but remained relatively constant over the subsequent 120 min examined. Dehydrogenase activity was not detectable in AP-3 ascospores but was measurable in germinating ascospores.

Fungal Proteins↗
PubMed1975

The possible role of pancreatic proteases in the turnover of intestinal brush border proteins.

1. Intestinal brush border enzymes have heterogeneous rates of turnover, the largest proteins having the fastest turnover. Since the membrane faces the intestinal lumen, the effects of pancreatic factors were examined in mediating this turnover. Surgical subtotal pancreatectomy was used as an experimental model to study the turnover of brush border proteins in the absence of most pancreatic secretions. 2. Subtotal (95%) pancreatectomy of rats was found to cause elevations by about 50% of total activity and specific activities of certain brush border enzymes (maltase, sucrase, lactase), but not of others (alkaline phosphatase, trehalase). Rats were judged to be functionally deficient in pancreatic proteolytic enzymes (a) by demonstration of vitamin B-12 malabsorption, which was corrected by trypsin, and (b) by the finding of only about 20% of proteolytic activity appearing in the lumen after a test meal when compared to control. 3. To measure protein turnover in vivo the method of double labelling was used, where [3H]- and [14C]valine were administered intraduodenally in sequence 10 h apart. With this technique, a high 3H/14C ratio is correlated with rapid turnover. Proteins with apparent molecular weights of about 200 000-270 000 were found to turn over more rapidly than smaller proteins. 3H/14C ranged from 4.7 to 6.2 in animals without pancreatic insufficiency. In the face of decreased pancreatic proteolysis, the 3H/14C ratio was 2.3-3.1, similar to that of proteins with a slow half life. 4. Estimates of relative synthetic rates of large brush border proteins were lower than normal in pancreatectomized animals, but were constant over the period of the labelling experiment. The high enzyme levels in the face of lower synthetic rates confirms that, at the new steady rate, degradation rates must be slower for large brush border proteins in pancreatic insufficiency. 5. In vitro, using purified brush borders, unfractionated pancreatic enzymes were found to remove sucrase, maltase and lactase, but not alkaline phosphatase and trehalase. The enzyme most potent in this respect was the pancreatic protease, elastase. Non-proteolytic enzymes (amylase, lipase, phospholipase A) were inactive in removing enzyme from the brush border. The addition of elastase to pancreatectomized animals in vivo restored the rapid turnover rate of large brush border proteins. 6. A model is thus proposed for the normal catabolism of some large intestinal brush border proteins. It is suggested that the surface of intestinal absorptive cells is being constantly remodelled, and that certain surface enzymes are in part removed from the membrane by the action of pancreatic proteases. A possible special role for elastase is suggested.

Alkaline Phosphatase↗
PubMed1976

Increase of enzyme activities in Neurospora crassa during incubation at low temperatures.

The effect of lowering the incubation temperature of sucrose-grown cultures of Neurospora crassa on the level of various enzyme activities was investigated. Of twelve inducible/derepressible activities studied, three, in addition to glycerol kinase, were found to increase during 48 h of incubation at 4-6 degrees C: trehalase (increase in specific activity of 3-10-fold), beta-glucosidase (6-12-fold) and beta-N-acetylglucosaminidase (4 to 6-fold). The maximum increases occurred at 6 degrees C and no increases took place in mycelia incubated at 0 degrees C. The kinetics of the changes in activity were markedly different from those observed previously with glycerol kinase. The increases were inhibited by cycloheximide. Trehalase, beta-glucosidase and beta-N-acetylglucosaminidase activities were not rapidly lost when cultures incubated at 6 degrees C were returned to 26 degrees C.

Acetylglucosaminidase↗
PubMed1988

Intestinal brush border membrane-bound disaccharidases of the American alligator, Alligator mississippiensis.

1. The disaccharidase activities of the small intestines of American alligators (Alligator mississippiensis) were studied in epithelial scrapes and brush-border membrane preparations. 2. Maltase, isomaltase and trehalase activities were found. Activities of these enzymes were higher in the proximal small intestine and decreased distally. 3. Disaccharidase activities were enriched 12-15 times in brush-border membrane preparations, compared with mucosa/enterocyte crude homogenates and were co-enriched with the brush-border membrane marker alkaline phosphatase. 3. The pH optima were: maltase 6.5; isomaltase 5.6; and trehalase 5.8. The Q10 of maltase, the most active enzyme, was equal to 1.82. 4. In reptiles, as in mammals, disaccharidase activities may be correlated with feeding habits. The co-occurrence of sucrase and isomaltase may not be a common feature of vertebrates.

Alligators and Crocodiles↗
PubMed2002

The function of trehalose biosynthesis in plants.

Trehalose (alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside) occurs in a large variety of organisms, ranging from bacteria to invertebrate animals, where it serves as an energy source or stress protectant. Until recently, only few plant species, mainly desiccation-tolerant 'resurrection' plants, were considered to synthesise trehalose. Instead of trehalose, most other plants species accumulate sucrose as major transport sugar and during stress. The ability to synthesize sucrose has probably evolved from the cyanobacterial ancestors of plastids and may be linked to photosynthetic function. Although most plant species do not appear to accumulate easily detectable amounts of trehalose, the discovery of genes for trehalose biosynthesis in Arabidopsis and in a range of crop plants suggests that the ability to synthesise trehalose is widely distributed in the plant kingdom. The apparent lack of trehalose accumulation in these plants is probably due to the presence of trehalase activity. After inhibition of trehalase, trehalose synthesis can be detected in Arabidopsis. Since trehalose induces metabolic changes, such as an accumulation of storage carbohydrates, rapid degradation of trehalose may be required to prevent detrimental effects of trehalose on the regulation of plant metabolism. In addition, the precursor of trehalose, trehalose-6-phosphate, is probably involved in the regulation of developmental and metabolic processes in plants.

Carbon↗
PubMed2001

Development of disaccharidase activity in the small intestine of broiler chickens.

1. The changes in disaccharidase activity in the small intestine of broiler chickens were investigated in isolated enterocytes on d 18 of embryonic development and d 1, 7, 21, 35 and 56 after hatching. 2. The specific activities of maltase, lactase and trehalase were greatest on d 18 of embryonic development. After hatching, maltase specific activity gradually decreased until d 18. 3. After d 7 postnatally only traces of lactase and trehalase activity were found in the enterocytes. 4. Significant sucrase activity was found on d 18 of embryonic development and the activity of this enzyme increased 2-fold after hatch and remained generally constant up to d 35, after which the enzyme specific activity declined.

Animals↗
PubMed1987

Disaccharidase activity in intestine epithelium microvilli membranes of lambs during the first month after birth.

Disaccharidase activity was studied in microvilli membranes of enterocytes isolated from duodenum, jejunum and ileum of lambs at an age of 1, 7 and 23 days. A maximum of lactase activity was observed on the 7th day compared to activity on 1st and 23rd day after parturition and a decrease in enzyme activity on the 23rd day compared to activity on the 7th day. Differences, however, were significant only in respect to activity in ileum. A significant increase of maltase activity in ileum and jejunum was established on the 7th and 23rd day compared to activity on the 1st day after parturition. Trehalase activity attained a maximum in all the three intestine divisions, consequently it subsided with no statistically significant differences. Lactase activity in ileum was significantly lower compared to activity in jejunum of lambs at an age of 1 and 23 days. A marked decrease of maltase activity in distal direction was found only on 1 day-old lambs. No significant alterations were observed in trehalase activity along the small intestine of lambs of the three age groups.

Animals↗
PubMed2003

Different roles for the stress-activated protein kinase pathway in the regulation of trehalose metabolism in Schizosaccharomyces pombe.

The Wis1p-Sty1p mitogen-activated protein kinase cascade is a major signalling system in the fission yeast Schizosaccharomyces pombe for a wide range of stress responses. It is known that trehalose functions as a protective metabolite to counteract deleterious effects of environmental stresses. Herein it is reported that the expression of genes related to trehalose metabolism in S. pombe, ntp1(+) (neutral trehalase) and tps1(+) [trehalose-6-phosphate (T6P) synthase], is partially regulated by the Sty1p kinase under salt-induced osmotic stress and conditions of slight oxidative stress and is fully dependent on this kinase under severe oxidative stress. This control is carried out through transcription factors Atf1p/Pcr1p during osmotic stress and through Pap1p during exposure to low levels of oxidative stress. However, all three transcription factors are needed for gene expression under conditions of extreme oxidative stress. In addition, a role for Sty1p in the modulation of post-transcriptional activation of trehalase mediated by Pka1p/Sck1p kinases, as well as in the activity of T6P synthase under such stressful conditions has been demonstrated. These results reveal a novel dual action of the Wis1p-Sty1p pathway in the regulation of trehalose metabolism in fission yeast.

Activating Transcription Factors↗
PubMed1996

Improved method for the preparative synthesis of labeled trehalose of high specific activity by Escherichia coli.

We report an improvement of a published procedure using Escherichia coli to synthesize 14C-labeled trehalose from [14C]glucose (B. Brand and W. Boos, Appl. Environ. Microbiol. 55:2414-2415, 1989). Instead of inducing the expression of the trehalose-synthesizing enzymes encoded by the chromosomal genes otsAB by high osmolarity, we now induce their expression from a plasmid under normal growth conditions by the addition of IPTG (isopropyl-beta-D-thiogalactopyranoside). Instead of using a pgi zwf double mutant to prevent glucose utilization, we use a pgi::Tn10 insertion only. In addition to being defective in treA, which encodes a periplasmic trehalase, the strain is now also defective in treF, which encodes a newly discovered cytoplasmic trehalase. This strain is genetically stable; it has no growth defects; and after induction with IPTG, it will transform [14C]glucose to [14C]trehalose in minimal medium without any carbon source under aerobic conditions at a rate of 3 nmol/min/10(9) cells. With the improved method, the overall yield of trehalose from glucose is about 80% and the process takes place without dilution of the specific radioactivity of the glucose residues. The accumulated trehalose is extracted from the bacteria by 70% hot ethanol and can easily be purified radiochemically by chromatographic techniques.

DNA Transposable Elements↗
PubMed1997

Trehalose induces antagonism towards Pythium debaryanum in Pseudomonas fluorescens ATCC 17400.

Pseudomonas fluorescens ATCC 17400 shows in vitro activity against Pythium debaryanum under conditions of iron limitation. A lacZ reporter gene introduced by transposon mutagenesis into the P. fluorescens ATCC 17400 trehalase gene (treA) was induced by a factor released by the phytopathogen Pythium debaryanum. The induction of the lacZ gene was lost upon treatment of the Pythium supernatant with commercial trehalase. A trehalose concentration as low as 1 microM could induce the expression of treA. The mutation did not affect the wild-type potential for fungus antagonism but drastically decreased the osmotolerance of the mutant in liquid culture and suppressed the ability of P. fluorescens ATCC 17400 to utilize trehalose as a carbon source. A subsequent transposon insertion in treP, one of the trehalose phosphotransferase genes upstream of treA, silenced the lacZ gene. This double mutant restricted fungal growth only under conditions of high osmolarity, which probably results in internal trehalose accumulation. These data confirm the role of the disaccharide trehalose in osmotolerance, and they indicate its additional role as an initiator of or a signal for fungal antagonism.

Amino Acid Sequence↗
PubMed2004

Two distinct pathways for trehalose assimilation in the yeast Saccharomyces cerevisiae.

The yeast Saccharomyces cerevisiae can synthesize trehalose and also use this disaccharide as a carbon source for growth. However, the molecular mechanism by which extracellular trehalose can be transported to the vacuole and degraded by the acid trehalase Ath1p is not clear. By using an adaptation of the assay of invertase on whole cells with NaF, we showed that more than 90% of the activity of Ath1p is extracellular, splitting of the disaccharide into glucose. We also found that Agt1p-mediated trehalose transport and the hydrolysis of the disaccharide by the cytosolic neutral trehalase Nth1p are coupled and represent a second, independent pathway, although there are several constraints on this alternative route. First, the AGT1/MAL11 gene is controlled by the MAL system, and Agt1p was active in neither non-maltose-fermenting nor maltose-inducible strains. Second, Agt1p rapidly lost activity during growth on trehalose, by a mechanism similar to the sugar-induced inactivation of the maltose permease. Finally, both pathways are highly pH sensitive and effective growth on trehalose occurred only when the medium was buffered at around pH 5.0. The catabolism of trehalose was purely oxidative, and since levels of Ath1p limit the glucose flux in the cells, batch cultures on trehalose may provide a useful alternative to glucose-limited chemostat cultures for investigation of metabolic responses in yeast.

Biological Transport↗
PubMed1986

Transport of trehalose in Salmonella typhimurium.

We have studied trehalose uptake in Salmonella typhimurium and the possible involvement of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) in this process. Two transport systems could recognize and transport trehalose, the mannose PTS and the galactose permease. Uptake of trehalose via the latter system required that it be expressed constitutively (due to a galR or galC mutation). Introduction of a ptsM mutation, resulting in a defective IIMan/IIIMan system, in S. typhimurium strains that grew on trehalose abolished growth on trehalose. A ptsG mutation, eliminating IIGlc of the glucose PTS, had no effect. In contrast, a crr mutation that resulted in the absence of IIIGlc of the glucose PTS prevented growth on trehalose. The inability of crr and also cya mutants to grow on trehalose was due to lowered intracellular cyclic AMP synthesis, since addition of extracellular cyclic AMP restored growth. Subsequent trehalose metabolism could be via a trehalose phosphate hydrolase, if trehalose phosphate was formed via the PTS, or trehalase. Trehalose-grown cells contained trehalase activity, but we could not detect phosphoenolpyruvate-dependent phosphorylation of trehalose in toluenized cells.

Bacterial Proteins↗
PubMed1981

Differential identification of Mycobacterium fortuitum and Mycobacterium chelonei.

Mycobacterium fortuitum and Mycobacterium chelonei are distinguished unambiguously by the combined use of five test characters: nitrate reductase, beta-glucosidase, acid production from fructose, penicillinase, and trehalase. Typically, M. fortuitum was nitrate reductase positive, beta-glucosidase positive; M. chelonei was nitrate reductase negative, beta-glucosidase negative, penicillinase positive, and trehalase positive and did not produce acid from fructose.

Fructose↗
PubMed1979

The physiological effects of restrictive environmental conditions on Dictyostelium discoideum spore germination.

Spores may be reversibly activated by the application of heat, dimethyl sulfoxide, urea, or ethylene glucol. Severe changes in four environmental variables (high osmotic pressure, low oxygen tension, low or high pH, and low or high temperature) interfere with the germination process. Spores at the end of the postactivation lag phase of germination were usually deactivated if exposed to severe environmental conditions and thus did not swell; spores in the swelling and oxygen uptake which began during spore activation was primarily attributable to a cyanide-sensitive pathway and secondarily to a salicylhydroxamic acid (SHAM) sensitive pathway. Inhibition of the SHAM-sensitive pathway did not cause spore deactivation while the addition of cyanide resulted in rapid spore deactivation. Treatment of activated spores with azide or environmental shifts also resulted in inhibition of oxygen uptake and spore deactivation. Deactivating spores did not demonstrate the amino acid incorporation, uridine incorporation, and expression of trehalase activity which is found in the later stages of germinating control spores. Protein synthesis inhibitors did not cause spore deactivation or a decrease in oxygen uptake but they inhibited amino acid incorporation and the expression trehalase activity in swollen spores. It is concluded that control of respiratory activity is involved in regulation of reversible activation.

Azides↗
PubMed1988

Effect of hormones on hydrolase activities and DNA synthesis in kidney of the developing mouse.

The postnatal development of brush border enzyme activities, namely maltase, trehalase, alkaline phosphatase, gamma-glutamyltranspeptidase, and leucylnaphthylamidase, as well as the ontogenic profile of DNA synthesis has been determined in the mouse kidney. In addition, these parameters were evaluated following daily administration of hormones during 3 days to 8-day-old mice. Insulin or epidermal growth factor induced a 34% increase of maltase activity over that of 11-day-old controls. Trehalase activity was precociously and significantly augmented by cortisone alone or combined with thyroxine (p less than 0.05), although thyroxine alone had no influence. Only epidermal growth factor had a significant effect on alkaline phosphatase activity. gamma-Glutamyltranspeptidase activity was significantly decreased when insulin and thyroxine were given simultaneously, but was not modified by any of the hormones injected separately. The level of leucylnaphthylamidase activity was enhanced by 70% after cortisone injection, but it was significantly reduced by thyroxine injected in combination with insulin or cortisone. The incorporation of [3H]thymidine into DNA was increased by 107% after epidermal growth factor administration, but it was decreased by 33% after the cortisone treatment. In spite of this precocious reduction, the level of incorporation was still 2 times higher than that in adult mice. These results show that hormones act separately or in cooperation to accelerate or retard the maturation of the suckling mouse kidney.

Alkaline Phosphatase↗
PubMed2004

Rapid induction of GATA transcription factors in developing mouse intestine following glucocorticoid administration.

In the developing intestine, transcription of alpha-glucosidase genes such as sucrase-isomaltase and trehalase is stimulated by glucocorticoid administration. The consequent increase of their respective mRNAs is characterized by a 12-h lag, suggesting that the response to glucocorticoids represents a secondary effect. We hypothesized that the primary response of the tissue to glucocorticoids includes induction of one or more intestinal transcription factors. To investigate this hypothesis, we identified a region in the mouse trehalase promoter (located at nucleotides -406 to -377 from the transcription start site) with potential binding sites for three transcription factors: Cdx-2, GATA, and C/EBP. Gel shifts were performed using labeled oligonucleotides from this region with nuclear extracts from jejunums of either control 8-day-old mouse pups or littermates treated with dexamethasone (DEX) 4 h before death. A specific shifted band was observed with DEX extracts but not with control extracts. Supershift assays indicated the presence of GATA-4 and GATA-6 but not GATA-5 nor Cdx-2, C/EBP alpha, C/EBP beta, or C/EBP delta. GATA binding was further implicated by competition studies with mutated oligonucleotides. Finally, Western blot analysis showed GATA-4 and GATA-6 proteins in DEX but not control nuclear extracts. For GATA-4, the same pattern was demonstrated with whole cell extracts and with the cytosol fraction. We conclude that expression of GATA-4 and GATA-6 proteins in the suckling mouse jejunum is stimulated by DEX. This novel finding constitutes an important first step in understanding the molecular mechanism of glucocorticoid action on the developing intestine.

Animals↗