Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.

Kopp, Meinrad; Müller, Hannelore; Holzer, Helmut

doi:10.1016/s0021-9258(18)53463-3

Cited by 130 publications

(11 citation statements)

References 51 publications

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“…The term 'stationary phase' should be definitely avoided in designating this panel of genes (Werner Washburne et al, 1996), since they were clearly induced much earlier than the 'post-diauxic shift' SSA3 gene (Boorstein and Craig, 1990) and the truly 'stationary phase' SNZ1 gene (Braun et al, 1996). Moreover, the specific induction of this class of genes while glucose was still abundant in the medium, and their maximal expression at the onset of the diauxic shift, argued against the claim that these genes are under 'catabolic repression' (Vuorio et al, 1993;Kopp et al, 1993;Nwaka et al, 1995a, b;Hardy et al, 1994;Winderickx et al, 1996), since typical glucose-repressed genes are solely derepressed after the complete exhaustion of glucose from the medium (Ronne, 1995;De Risi et al, 1997). Even though catabolite repression is indeed inappropriate, we noticed a strong negative correlation between initial glucose concentration and reserve carbohydrate metabolism, but we do not yet have a clear explanation for this specific 'glucose effect'.…”

Section: Discussionmentioning

confidence: 99%

Dynamic responses of reserve carbohydrate metabolism under carbon and nitrogen limitations inSaccharomyces cerevisiae

Parrou

Enjalbert

Plourde

et al. 1999

Yeast

144

134

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The dynamic responses of reserve carbohydrates with respect to shortage of either carbon or nitrogen source was studied to obtain a sound basis for further investigations devoted to the characterization of mechanisms by which the yeast Saccharomyces cerevisiae can cope with nutrient limitation during growth. This study was carried out in well‐controlled bioreactors which allow accurate monitoring of growth and frequent sampling without disturbing the culture. Under glucose limitation, genes involved in glycogen and trehalose biosynthesis (GLG1, GSY1, GSY2, GAC1, GLC3, TPS1 ), in their degradation (GPH1, NTH1 ), and the typical stress‐responsive CTT1 gene were coordinately induced in parallel with glycogen, when the growth has left the pure exponential phase and while glucose was still plentiful in the medium. Trehalose accumulation was delayed until the diauxic shift, although TPS1 was induced much earlier, due to hydrolysis of trehalose by high trehalase activity. In contrast, under nitrogen limitation, both glycogen and trehalose began to accumulate at the precise time when the nitrogen source was exhausted from the medium, coincidentally with the transcriptional activation of genes involved in their metabolism. While this response to nitrogen starvation was likely mediated by the stress‐responsive elements (STREs) in the promoter of these genes, we found that these elements were not responsible for the co‐induction of genes involved in reserve carbohydrate metabolism during glucose limitation, since GLG1, which does not contain any STRE, was coordinately induced with GSY2 and TPS1. Copyright © 1999 John Wiley & Sons, Ltd.

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Section: Discussionmentioning

confidence: 99%

Dynamic responses of reserve carbohydrate metabolism under carbon and nitrogen limitations inSaccharomyces cerevisiae

Parrou

Enjalbert

Plourde

et al. 1999

Yeast

144

134

View full text Add to dashboard Cite

show abstract

“…Trehalases (α,α-trehalose-1-C-glukohydrolases) are part of the Glycoside hydrolase family 37 (EC 3.2.1.28) of O-Glycosyl hydrolases (EC 3.2.1.) which includes enzymes with mutual trehalase activity identified in many different organisms, from bacteria to fungi, plants and animals (Elbein 1974, App and Holzer 1989, Kopp et al 1993. Trehalases are conserved enzymes that catalyze the hydrolysis of one of two glycoside bonds of trehalose (Kopp et al 1993, Kopp et al 1994, Nwaka and Holzer 1998, Bock et al 1983).…”

Section: Introductionmentioning

confidence: 99%

“…which includes enzymes with mutual trehalase activity identified in many different organisms, from bacteria to fungi, plants and animals (Elbein 1974, App and Holzer 1989, Kopp et al 1993. Trehalases are conserved enzymes that catalyze the hydrolysis of one of two glycoside bonds of trehalose (Kopp et al 1993, Kopp et al 1994, Nwaka and Holzer 1998, Bock et al 1983). In the yeast S. cerevisiae, trehalose can be hydrolyzed by the neutral trehalases Nth1 and Nth2, which share 73 % identity, and by the acid trehalase Ath1 (Thevelein 1984a, Thevelein 1984b, Nwaka et al 1995.…”

Section: Introductionmentioning

confidence: 99%

Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein

Alblova

Smidova²,

Kalabova³

et al. 2019

Physiol Res

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Neutral trehalase 1 (Nth1) from Saccharomyces cerevisiae catalyzes disaccharide trehalose hydrolysis and helps yeast to survive adverse conditions, such as heat shock, starvation or oxidative stress. 14-3-3 proteins, master regulators of hundreds of partner proteins, participate in many key cellular processes. Nth1 is activated by phosphorylation followed by 14-3-3 protein (Bmh) binding. The activation mechanism is also potentiated by Ca(2+) binding within the EF-hand-like motif. This review summarizes the current knowledge about trehalases and the molecular and structural basis of Nth1 activation. The crystal structure of fully active Nth1 bound to 14-3-3 protein provided the first high-resolution view of a trehalase from a eukaryotic organism and showed 14-3-3 proteins as structural modulators and allosteric effectors of multi-domain binding partners.

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“…The results showed that the appressorium collapsed rates of the Δ MaAreB strain were increased significantly compared with that from the WT or CP strain ( Figure 8 A). The glycerol produced by lipids in appressorium can enhance turgor pressure and promote the penetration of appressorium [ 41 , 43 , 44 ]. qRT-PCR analyses showed that the transcription of glycerol synthesis-related genes, MaGPD1 and MaMPL1 decreased significantly in Δ MaAreB ( Figure 8 B).…”

Section: Resultsmentioning

confidence: 99%

MaAreB, a GATA Transcription Factor, Is Involved in Nitrogen Source Utilization, Stress Tolerances and Virulence in Metarhizium acridum

Zhang

Xia

et al. 2021

JoF

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The nitrogen catabolite repression (NCR) pathway is involved in nitrogen utilization, in which the global GATA transcription factor AreA plays an indispensable role and has been reported in many fungi. However, relatively few studies are focused on AreB, another GATA transcription factor in the NCR pathway and the functions of AreB are largely unknown in entomopathogenic fungi. Here, we characterized MaAreB in the model entomopathogenic fungus Metarhizium acridum. Sequence arrangement found that MaAreB had a conserved GATA zinc finger DNA binding domain and a leucine zipper domain. Disruption of MaAreB affected the nitrogen utilization and led to decelerated conidial germination and hyphal growth, decreased conidial yield, and lower tolerances to UV-B irradiation and heat-shock. Furthermore, the MaAreB mutant (ΔMaAreB) exhibited increased sensitivity to CFW (Calcofluor white), decreased cell wall contents (chitin and β-1,3-glucan) and reduced expression levels of some genes related to cell wall integrity, indicating that disruption of MaAreB affected the cell wall integrity. Bioassays showed that the virulence of the ΔMaAreB strain was decreased in topical inoculation but not in intra-hemocoel injection. Consistently, deletion of MaAreB severely impaired the appressorium formation and reduced the turgor pressure of appressorium. These results revealed that MaAreB regulated fungal nitrogen utilization, cell wall integrity and biological control potential, which would contribute to the functional characterization of AreB homologous proteins in other insect fungal pathogens, and even filamentous fungi.

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Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.

Cited by 130 publications

References 51 publications

Dynamic responses of reserve carbohydrate metabolism under carbon and nitrogen limitations inSaccharomyces cerevisiae

Dynamic responses of reserve carbohydrate metabolism under carbon and nitrogen limitations inSaccharomyces cerevisiae

Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein

MaAreB, a GATA Transcription Factor, Is Involved in Nitrogen Source Utilization, Stress Tolerances and Virulence in Metarhizium acridum

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