Synthesis and maturation of the yeast vacuolar enzymes carboxypeptidase Y and aminopeptidase I
| Autor: | E.W. Jones, E.J.M. Al, Henk F. Tabak, Ben Distel |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Glycosylation Saccharomyces cerevisiae Biophysics Cathepsin A Carboxypeptidases Vacuole Aminopeptidases Biochemistry chemistry.chemical_compound Biosynthesis Structural Biology Genetics RNA Messenger chemistry.chemical_classification Methionine biology Protoplasts RNA Fungal Tunicamycin biology.organism_classification Carboxypeptidase Organoids Enzyme chemistry Protein Biosynthesis Mutation Vacuoles biology.protein Protein Processing Post-Translational |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 741:128-135 |
| ISSN: | 0167-4781 |
| Popis: | We have studied the two vacuolar enzymes carboxypeptidase Y and aminopeptidase I from Saccharomyces cerevisiae with respect to biosynthesis, maturation and transfer from their site of synthesis into the organelle. The levels of translatable mRNA for these two proteins increase more than 10-fold at the end of the exponential growth period on glucose as carbon source and decrease again in the stationary phase. Two precursors of carboxypeptidase Y have been identified by in vivo pulse-labelling with [ 35 S]methionine. These differ in their amount of carbohydrate as shown by inhibition of N-linked glycosylation with tunicamycin. The first is a protein with an apparent molecular weight of 67 kDa, which can be converted into the mature 60-kDa protein via an intermediate of 69 kDa. In the pep4-3 mutant, which is disturbed in the maturation of several vacuolar enzymes (Hemmings, B.A., Zubenko, G.S., Hasilik, A. and Jones, E.W. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 435–439), the 69-kDa precursor accumulates in the vacuole. This suggests that the final proteolytic cleavage of carboxypeptidase Y can occur in the vacuole. |
| Databáze: | OpenAIRE |
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