title: Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae.
abstract: The disaccharide trehalose plays a critical role in yeast cell survival during conditions of environmental stress. The vacuole of the yeast Saccharomyces cerevisiae contains an enzyme, acid trehalase (ATH), that is capable of degrading trehalose. Recently, a gene required for ATH activity, ATH1, was cloned and sequenced [Destruelle et al., (1995) Yeast 11, 1015-1025]. The relationship between ATH1 and ATH, however, was not determined. We have purified ATH and shown that it is the ATH1 gene product; peptide sequences from the purified protein correspond to the deduced amino acid sequence of Ath1p. In addition, antiserum to Ath1p specifically recognizes purified ATH.
authors.affiliation: Section of Microbiology, University of California, Davis 95616, USA.
authors.forename: P
authors.initials: P
authors.lastname: Alizadeh
authors.forename: D J
authors.initials: DJ
authors.lastname: Klionsky
mesh_terms: D000595:Amino Acid Sequence; D000918:Antibody Specificity; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010957:Plasmids; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D014198:Trehalase / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; C097090:ATH1 protein, S cerevisiae; D014198:Trehalase