Co-purification of glucanase with acid trehalase-invertase aggregate in Saccharomyces cerevisiae.
An electrophoretically homogenous aggregate of acid trehalase, invertase and an unidentified 37-41 kDa protein was purified from Saccharomyces cerevisiae. N-terminal analysis of the protein revealed an amino acid sequence identical to that of Bgl2p (endo-beta-l,3-glucanase) of S. cerevisiae. Acid trehalase activity with co-eluted glucanase activity was observed from late growth phase through early stationary phase. Pools with high percentage of Bgl2p corresponded with high acid trehalase activity. A BGL2 deletion strain had lower acid trehalase activity. The 37-41 kDa protein represents Bgl2p which, besides imparting glucanase activity, could also be acting as a regulator for the acid trehalase activity by association in the enzyme aggregate.
Basu
Arghya
A
Biotechnology Division, Indian Institute of Chemical Biology, Kolkata 700 032, India.
Chaudhuri
Paramita
P
Malakar
Dipankar
D
Ghosh
Anil K
AK
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000302:isolation & purification*; D014198:Trehalase; D043324:beta-Fructofuranosidase
D029701:Saccharomyces cerevisiae Proteins; D043324:beta-Fructofuranosidase; D014198:Trehalase; C080389:BGL2 protein, S cerevisiae; D004693:Glucan Endo-1,3-beta-D-Glucosidase