Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae

FEBS Letters

Alizadeh, Parvaneh¹  Klionsky, Daniel J.¹ 

[1] Section of Microbiology, University of California, Davis, CA 95616, USA

关键词: Acid trehalase;    ATH1 gene;    Trehalose;    Vacuole;    Yeast;    ATH;    acid trehalase;    Endo H;    endo-β-N-acetylglucosaminidase H;    IEF;    isoelectric focusing;    NTH;    neutral trehalase;    PIPES;    piperazine-N;    N′-bis(2-ethanesulfonic acid);    PrA;    proteinase A;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    YNB;    yeast nitrogen base;    YPD;    1% bacto-yeast extract 2% bacto-peptone 2% dextrose;   

DOI  :  10.1016/0014-5793(96)00751-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown