Changes in the post-translational modification of lysosomal enzymes during development of Dictyostelium.
The form of post-translational modification present on two lysosomal enzymes--acid phosphatase and alpha-mannosidase--changes as part of the developmental program of Dictyostelium discoideum. Prior to 8 h of development, all enzyme molecules are of a single modification type (early form enzyme). Starting at 8 h of development, enzyme molecules with a second type of modification (late-form enzymes) begin to appear in the cell. We separated the early and late forms of these enzymes from each other by chromatography on DEAE-cellulose. We found that the change in protein modification affects the enzymes' in vitro properties. The early and late forms of both of these enzymes differ in thermostability and susceptibility to proteolytic inactivation. We also found that the late form of alpha-mannosidase is preferentially secreted. We suggest that by synthesizing molecules with a second form of modification, the cell confers new characteristics to its lysosomal enzymes.
D000135:Acid Phosphatase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D004023:Dictyostelium / Q000201:enzymology*; D004355:Drug Stability; D006358:Hot Temperature; D007700:Kinetics; D008247:Lysosomes / Q000201:enzymology*; D008361:Mannosidases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010447:Peptide Hydrolases; D011499:Protein Processing, Post-Translational; D043323:alpha-Mannosidase
D000135:Acid Phosphatase; D008361:Mannosidases; D043323:alpha-Mannosidase; D010447:Peptide Hydrolases