PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30007297-0 2018 The trehalose protective mechanism during thermal stress in Saccharomyces cerevisiae: the roles of Ath1 and Agt1. Trehalose 4-13 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 99-103 30007297-6 2018 By a similar mechanism, Ath1 would reach the cell surface to hydrolyze the external trehalose but only when the stress would be over. Trehalose 84-93 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 24-28 30007297-7 2018 Corroborating this conclusion, Ath1 activity in soluble cell-free extracts increased after 40 C adaptation but decreased when cells returned to 28 C. During 40 C, Ath1 is confined into vesicles, avoiding the cleavage of the outside trehalose. Trehalose 232-241 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 31-35 19703229-1 2009 Previous studies in the yeast Saccharomyces cerevisiae have proposed a vacuolar localization for Ath1, which is difficult to reconcile with its ability to hydrolyze exogenous trehalose. Trehalose 175-184 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 97-101 27510429-4 2016 Moreover, expression of the trehalose degradation-related genes NTH1 and NTH2 decreased at exponential phase in comparison with that at lag phase; compared with cells at lag phase, cells at stationary phase had higher expression of TPS1, ATH1, NTH1, and NTH2 but lower expression of TPS2. Trehalose 28-37 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 238-242 24951963-3 2014 Deleting ATH1 exerted a significant effect on trehalase activities and the degradation amount of intracellular trehalose during the first 30 min of prefermentation. Trehalose 111-120 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 9-13 24951963-4 2014 This finding indicates that acid trehalase (Ath1) plays a role in intracellular trehalose degradation. Trehalose 80-89 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 44-48 19703229-5 2009 Finally, the physiological significance of the cell-surface localization of Ath1 was established by showing that fusion of the signal peptide of invertase to N-terminal truncated Ath1 allowed the ath1Delta mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevented growth of this mutant on trehalose. Trehalose 364-373 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 179-183 19703229-5 2009 Finally, the physiological significance of the cell-surface localization of Ath1 was established by showing that fusion of the signal peptide of invertase to N-terminal truncated Ath1 allowed the ath1Delta mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevented growth of this mutant on trehalose. Trehalose 364-373 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 179-183 19703229-5 2009 Finally, the physiological significance of the cell-surface localization of Ath1 was established by showing that fusion of the signal peptide of invertase to N-terminal truncated Ath1 allowed the ath1Delta mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevented growth of this mutant on trehalose. Trehalose 224-233 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 76-80 19703229-5 2009 Finally, the physiological significance of the cell-surface localization of Ath1 was established by showing that fusion of the signal peptide of invertase to N-terminal truncated Ath1 allowed the ath1Delta mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevented growth of this mutant on trehalose. Trehalose 224-233 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 179-183 19703229-5 2009 Finally, the physiological significance of the cell-surface localization of Ath1 was established by showing that fusion of the signal peptide of invertase to N-terminal truncated Ath1 allowed the ath1Delta mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevented growth of this mutant on trehalose. Trehalose 224-233 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 179-183 19703229-5 2009 Finally, the physiological significance of the cell-surface localization of Ath1 was established by showing that fusion of the signal peptide of invertase to N-terminal truncated Ath1 allowed the ath1Delta mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevented growth of this mutant on trehalose. Trehalose 364-373 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 76-80 19520725-0 2009 The three trehalases Nth1p, Nth2p and Ath1p participate in the mobilization of intracellular trehalose required for recovery from saline stress in Saccharomyces cerevisiae. Trehalose 93-102 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 38-43 18065618-7 2008 However, when the Ath1p-dependent mobilization of trehalose identified in this study was impaired, glycogen was mobilized earlier and faster, indicating a fine-tuning control in carbon storage management during periods of carbon and energy restriction. Trehalose 50-59 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 18-23 19126402-2 2009 ATH1, and NTH1 hydrolyze trehalose to glucose to provide energy and assist in recovery from stress. Trehalose 25-34 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 0-4 19160808-2 2008 Two enzymes are capable of hydrolyzing trehalose: a neutral trehalase (NTH1) and an acidic trehalase (ATH1). Trehalose 39-48 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 102-106 18065618-0 2008 New insights into trehalose metabolism by Saccharomyces cerevisiae: NTH2 encodes a functional cytosolic trehalase, and deletion of TPS1 reveals Ath1p-dependent trehalose mobilization. Trehalose 18-27 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 144-149 18065618-0 2008 New insights into trehalose metabolism by Saccharomyces cerevisiae: NTH2 encodes a functional cytosolic trehalase, and deletion of TPS1 reveals Ath1p-dependent trehalose mobilization. Trehalose 160-169 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 144-149 8647289-8 1996 Our results show that the vacuolar acid trehalase Ath1p is necessary for the phenotype of growth on trehalose, i.e. trehalose utilization, in contrast to cytosolic neutral trehalase Nth1p which is necessary for intracellular degradation of trehalose. Trehalose 116-125 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 50-55 15128531-2 2004 However, the molecular mechanism by which extracellular trehalose can be transported to the vacuole and degraded by the acid trehalase Ath1p is not clear. Trehalose 56-65 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 135-140 17673210-4 2007 The full-length AtTRE1, when expressed in yeast can functionally substitute for the extracellularly active trehalase Ath1p, by sustaining the growth of an ath1 null mutant strain on trehalose and at pH 4.8. Trehalose 182-191 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 117-122 17475771-4 2007 Hydrolysis of trehalose in yeast depends on neutral trehalase and acid trehalase (Ath1). Trehalose 14-23 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 82-86 17475771-5 2007 Ath1 resides and functions in the vacuole; however, it appears to catalyze the hydrolysis of extracellular trehalose. Trehalose 107-116 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 0-4 8647289-0 1996 Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. Trehalose 73-82 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 16-20 8647289-6 1996 Experiments with diploid strains heterozygous for delta ath1 show a gene dosage effect for the ATH1 gene for growth on trehalose. Trehalose 119-128 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 56-60 8647289-6 1996 Experiments with diploid strains heterozygous for delta ath1 show a gene dosage effect for the ATH1 gene for growth on trehalose. Trehalose 119-128 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 95-99 8647289-8 1996 Our results show that the vacuolar acid trehalase Ath1p is necessary for the phenotype of growth on trehalose, i.e. trehalose utilization, in contrast to cytosolic neutral trehalase Nth1p which is necessary for intracellular degradation of trehalose. Trehalose 100-109 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 50-55 8647289-8 1996 Our results show that the vacuolar acid trehalase Ath1p is necessary for the phenotype of growth on trehalose, i.e. trehalose utilization, in contrast to cytosolic neutral trehalase Nth1p which is necessary for intracellular degradation of trehalose. Trehalose 116-125 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 50-55 8633854-4 1996 The delta ath1 strain accumulated greater levels of cellular trehalose and grew to a higher cell density than the isogenic wild-type strain. Trehalose 61-70 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 10-14 8633854-5 1996 In addition, the elevated levels of trehalose in the delta ath1 strain correlated with increased tolerance to dehydration, freezing, and toxic levels of ethanol. Trehalose 36-45 alpha,alpha-trehalase ATH1 Saccharomyces cerevisiae S288C 59-63