Yeast trehalases: Two enzymes, one catalytic mission

Maicas, Sergi; Guirao-Abad, José P.; Argüelles, Juan-Carlos

doi:10.1016/j.bbagen.2016.04.020

Cited by 15 publications

(18 citation statements)

References 48 publications

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“…Yeast neutral and acid trehalases exhibit sharp differences in subcellular localization, being located in the cytosol and vacuoles or cell wall, respectively (Maicas et al., 2016). In this study, we fused FgNTH and FgATH with the green fluoresecent protein gene GFP , and transformed FgNTH‐GFP and FgATH‐GFP constructs into Δ FgNTH and Δ FgATH , respectively.…”

Section: Resultsmentioning

confidence: 99%

“…However, the targets of VMA at gene level and its molecular mechanism of reducing DON contamination are poorly understood. Yeasts and filamentous fungi usually contain two types of trehalase that can be distinguished based on their cellular location, physiological role, and regulatory mechanism: the so‐called neutral trehalases and acid trehalases (Maicas et al., 2016). In the current study, we identified FgNTH and FgATH in F .…”

Section: Discussionmentioning

confidence: 99%

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Mechanism of validamycin A inhibiting DON biosynthesis and synergizing with DMI fungicides against Fusarium graminearum

Bian

Duan

Xiu

et al. 2021

Molecular Plant Pathology

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Deoxynivalenol (DON) is a vital virulence factor of Fusarium graminearum, which causes Fusarium head blight (FHB). We recently found that validamycin A (VMA), an aminoglycoside antibiotic, can be used to control FHB and inhibit DON contamination, but its molecular mechanism is still unclear. In this study, we found that both neutral and acid trehalase (FgNTH and FgATH) are the targets of VMA in F. graminearum, and the deficiency of FgNTH and FgATH reduces the sensitivity to VMA by 2.12‐ and 1.79‐fold, respectively, indicating that FgNTH is the main target of VMA. We found FgNTH is responsible for vegetative growth, FgATH is critical to sexual reproduction, and both of them play an important role in conidiation and virulence in F. graminearum. We found that FgNTH resided in the cytoplasm, affected the localization of FgATH, and positively regulated DON biosynthesis; however, FgATH resided in vacuole and negatively regulated DON biosynthesis. FgNTH interacted with FgPK (pyruvate kinase), a key enzyme in glycolysis, and the interaction was reduced by VMA; the deficiency of FgNTH affected the localization of FgPK under DON induction condition. Strains with a deficiency of FgNTH were more sensitive to demethylation inhibitor (DMI) fungicides. FgNTH regulated the expression level of FgCYP51A and FgCYP51B by interacting with FgCYP51B. Taken together, VMA inhibits DON biosynthesis by targeting FgNTH and reducing the interaction between FgNTH and FgPK, and synergizes with DMI fungicides against F. graminearum by decreasing FgCYP51A and FgCYP51B expression.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Mechanism of validamycin A inhibiting DON biosynthesis and synergizing with DMI fungicides against Fusarium graminearum

Bian

Duan

Xiu

et al. 2021

Molecular Plant Pathology

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“…Both types of organisms contain two kinds of enzymes, which display sharp differences in biochemical features, subcellular location and physiological roles. In insects, trehalase‐1 (tre‐1) is a soluble enzyme present in the hemolymph, midgut goblet cells and eggs, whereas the yeast neutral trehalase (Ntc1p/Nth1p) is a cytosolic enzyme regulated by cAMP‐PKA phosphorylation 5,22,23 . In turn, the insect trehalase‐2 (tre‐2) is a membrane‐bound isozyme identified in flight muscle, ovary cells, spermatophore, midgut and brain tissue 5,8 .…”

Section: Validamycin a And The Trehalase–trehalose System In Fungimentioning

confidence: 99%

“…The interconnection between the two distinct trehalases appears to be complex. However, the yeast trehalases share a strict specificity for trehalose as sole substrate, based on the presence of an (α/α) 6 toroid folding structure in the active centre and a catalytic mechanism of anomeric inversion 22,23 . Of note is the fact that some enzymatic components involved in the metabolism of trehalose, namely trehalose synthase, trehalose phosphatase or external trehalase, have been considered as potential targets for the design of specific new fungicides and insecticides 5,14,17,23 …”

Section: Validamycin a And The Trehalase–trehalose System In Fungimentioning

confidence: 99%

“…Whenever possible, the disruption of trehalase gene(s) in the targeted insect or fungus must be performed, and the subsequent hypothetical phenotypes examined in detail. In this way, the homozygous atc1 null mutants of C. albicans show a decrease of hypha formation, infectivity and the capacity to produce biofilms 23 . (ii) A biochemical research.…”

Section: Some Suggestions and Implicationsmentioning

confidence: 99%

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Trehalase inhibition by validamycin A may be a promising target to design new fungicides and insecticides

García

Argüelles

2021

Pest Management Science

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The introduction of insecticides and fungicides in agriculture has improved crop yields and, consequently, the quality of life for many people, especially in what is widely considered as the ‘first world’. However, the indiscriminate use of dangerous chemical insecticides has led to pest resistance, human and animal poisoning and environmental pollution. Biochemical and genetic evidence concludes that the non‐reducing disaccharide trehalose plays an essential role in the pathobiology of many insects and fungi. Both organisms share identical pathway for trehalose biosynthesis (the TPS/TPP pathway), while a high degree of homology in their trehalose hydrolysis capacity (trehalase activities) has also been demonstrated. In the search for new, effective and environmentally sustainable compounds, a set of trehalase inhibitors has emerged as a potentially interesting antifungal and insecticidal target. In particular, the trehalose analogue, Validamycin A, which has a strong inhibitory effect on several trehalases, has been successfully introduced for the treatment of various diseases caused by insects and fungi. Herein, we review the main features of the specific interaction between Validamycin A and trehalase as well as the expected advantages of the applications based on trehalase inhibition as insecticides and fungicides. © 2021 Society of Chemical Industry.

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Two trehalose-hydrolyzing enzymes from Crenarchaeon Sulfolobus acidocaldarius exhibit distinct activities and affinities toward trehalose

Yuasa

Okamura

Kimura

et al. 2018

Appl Microbiol Biotechnol

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Two archaeal trehalase-like genes, Saci1250 and Saci1816, belonging to glycoside hydrolase family 15 (GH15) from the acidophilic Crenarchaeon Sulfolobus acidocaldarius were expressed in Escherichia coli. The gene products showed trehalose-hydrolyzing activities, and the names SaTreH1 and SaTreH2 were assigned to Saci1816 and Saci1250 gene products, respectively. These newly identified enzymes functioned within a narrow range of acidic pH values at elevated temperatures, which is similar to the behavior of Euryarchaeota Thermoplasma trehalases. SaTreH1 displayed high K and k values, whereas SaTreH2 had lower K and k values despite a high degree of identity in their primary structures. A mutation analysis indicated that two glutamic acid residues in SaTreH1, E374 and E574, may be involved in trehalase catalysis because SaTreH1 E374Q and E574Q showed greatly reduced trehalose-hydrolyzing activities. Additional mutations substituting G573 and H575 residues with serine and glutamic acid residues, respectively, to mimic the TVN1315 sequence resulted in a decrease in trehalase activity and thermal stability. Taken together, the results indicated that Crenarchaea trehalases adopt active site structures that are similar to Euryarchaeota enzymes but have distinct molecular features. The identification of these trehalases could extend our understanding of the relationships between the structure and function of GH15 trehalases as well as other family enzymes and will provide insights into archaeal trehalose metabolism.

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Yeast trehalases: Two enzymes, one catalytic mission

Cited by 15 publications

References 48 publications

Mechanism of validamycin A inhibiting DON biosynthesis and synergizing with DMI fungicides against Fusarium graminearum

Mechanism of validamycin A inhibiting DON biosynthesis and synergizing with DMI fungicides against Fusarium graminearum

Trehalase inhibition by validamycin A may be a promising target to design new fungicides and insecticides

Two trehalose-hydrolyzing enzymes from Crenarchaeon Sulfolobus acidocaldarius exhibit distinct activities and affinities toward trehalose

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