Effects of a post-translational modification mutation on different developmentally regulated glycosidases in Dictyostelium discoideum.
We have studied the effect of a post-translational modification mutation upon four developmentally regulated glycosidases of Dictyostelium discoideum. The presence of the modA mutation affects the intracellular level of these multimeric enzymes differently. The level of alpha-glucosidase is unaffected in the modA mutant. The mutant cell contains only a very small fraction of the wild type beta-glucosidase-1 activity. The alteration in modification renders beta-glucosidase-1 holoenzyme thermolabile and susceptible to degradation in vivo. alpha-Mannosidase-1 and N-acetylglucosaminidase are found at approximately 1/3 of the wild type level in the modA mutant. Degradation of holoenzyme does not appear to be responsible for the low level of these activities. We propose that alpha-mannosidase-1 and N-acetylglucosaminidase subunits are being degraded prior to subunit assembly. We conclude the modification bestows different properties upon the various glycosidases.
D000118:Acetylglucosaminidase / Q000235:genetics; D003513:Cycloheximide / Q000494:pharmacology; D004023:Dictyostelium / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D006026:Glycoside Hydrolases / Q000235:genetics*; D007700:Kinetics; D008361:Mannosidases / Q000235:genetics; D009154:Mutation; D009235:Myxomycetes / Q000201:enzymology*; D000520:alpha-Glucosidases / Q000235:genetics; D001617:beta-Glucosidase / Q000235:genetics
D003513:Cycloheximide; D006026:Glycoside Hydrolases; D008361:Mannosidases; D000520:alpha-Glucosidases; D001617:beta-Glucosidase; D000118:Acetylglucosaminidase