Correlation between stationary phase survival and acid trehalase activity in yeast.
The levels of two trehalose hydrolysing enzymes, acid trehalase (AT) and neutral trehalase (NT), have been investigated in Candida utilis at different stages of growth; in complete contrast to Saccharomyces cerevisiae, significant AT activity appears to be absent at all stages of growth studied in C. utilis. In addition, presence of only very low amounts of iso-aspartyl methyl transferase (IMT) activity at the onset of stationary phase and lower survival ability in early stationary phase in contrast to that of S. cerevisiae lend support to the ideas that (a) lower degree of survival of C. utilis in the stationary phase may be a direct consequence of inability to mobilise stored trehalose due to absence of intracellular AT and reduced levels of IMT activities and (b) trehalose may have a dual role vis-à-vis stress resistance in yeasts.
Roy
A
A
Department of Applied Biochemistry, Indian Institute of Chemical Biology, Calcutta, India.
Ghosh
A K
AK
D002175:Candida / Q000201:enzymology* / Q000254:growth & development*; D005656:Fungal Proteins / Q000378:metabolism; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D011496:Protein Methyltransferases / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000254:growth & development; D029701:Saccharomyces cerevisiae Proteins; D014198:Trehalase / Q000378:metabolism*
D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D012436:S-Adenosylmethionine; D011496:Protein Methyltransferases; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; C097090:ATH1 protein, S cerevisiae; D014198:Trehalase