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Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae
Author(s) -
Alizadeh Parvaneh,
Klionsky Daniel J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00751-x
Subject(s) - saccharomyces cerevisiae , trehalose , biochemistry , yeast , trehalase , gene product , biology , gene , vacuole , enzyme , chemistry , gene expression , cytoplasm
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 trehalose (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.