Role of glycosylation in secretion of yeast acid phosphatase.
The minimal glycosylation requirement for acid phosphatase secretion and activity was investigated using tunicamycin, an inhibitor of protein glycosylation, and a yeast mutant defective in the synthesis of oligosaccharide outer chains. The results obtained show that outer chain addition is not essential for secretion of active enzyme and that only 4 core chains, out of 8 normally attached to a protein subunit, are sufficient for enzyme transport to the periplasmic space. Enzyme forms with less than 4 chains were retained in membranes of endoplasmic reticulum. Secreted underglycosylated enzyme forms are partially or completely inactive.
Mrsa
V
V
Barbarić
S
S
Ries
B
B
Mildner
P
P
D000135:Acid Phosphatase / Q000378:metabolism*; D001692:Biological Transport; D050260:Carbohydrate Metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology*; D014415:Tunicamycin / Q000494:pharmacology
D005656:Fungal Proteins; D006023:Glycoproteins; D014415:Tunicamycin; D000135:Acid Phosphatase