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In  Trichoderma reesei , dolichyl phosphate mannose (dpm) synthase, a key enzyme in the O-glycosylation process, requires three proteins for full activity. In this study, the  dpm2  and  dpm3  genes coding for the DPMII and DPMIII subunits of  T. reesei  DPM synthase were cloned and functionally analyzed after expression in the  Saccharomyces cerevisiae dpm1Δ  [genotype (BY4743;  his3Δ1; /leu2Δ0; lys2Δ0; /ura3Δ0; YPR183w::kanMX4 ] mutant. It was found that apart from the catalytic subunit DPMI, the DPMIII subunit is also essential to form an active DPM synthase in yeast. Additional expression of the DPMII protein, considered to be a regulatory subunit of DPM synthase, decreased the enzymatic activity. We also characterized  S. cerevisiae  strains expressing the  dpm1 ,  2 ,  3  or  dpm1, 3  genes and analyzed the consequences of  dpm  expression on protein O-glycosylation  in vivo  and on the cell wall composition.

Cloning and functional analysis of the dpm2 and dpm3 genes from Trichoderma reesei expressed in a Saccharomyces cerevisiae dpm1Δ mutant strain