Phenotypic analysis of proteinase A mutants. Implications for autoactivation and the maturation pathway of the vacuolar hydrolases of Saccharomyces cerevisiae
| Autor: | M A Innis, Elizabeth W. Jones, J D Garman, J A Noble, Carol A. Woolford, Ming F. Tam |
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| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
animal structures Protease biology medicine.medical_treatment Mutant Saccharomyces cerevisiae Active site Cell Biology urologic and male genital diseases biology.organism_classification Biochemistry female genital diseases and pregnancy complications Enzyme chemistry Hydrolase medicine biology.protein Site-directed mutagenesis Molecular Biology Gene hormones hormone substitutes and hormone antagonists circulatory and respiratory physiology |
| Zdroj: | Journal of Biological Chemistry. 268:8990-8998 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(18)52969-0 |
| Popis: | We have isolated a number of mutants deficient in activity of the vacuolar hydrolase proteinase A (PrA). The mutations were sequenced and although they all map in the PEP4 gene, which encodes the precursor to PrA, three distinguishable phenotypes have surfaced. The properties of the pep4-7 missense mutant suggested that the activation of the precursor to proteinase A is due to an autocatalytic cleavage. PrA active site mutations were constructed and resulted in accumulation of PrA antigen in the inactive precursor form. Although protease B (PrB), another vacuolar hydrolase, is not required for the production of active PrA, the active form of PrA that accumulates in a strain lacking PrB is larger than that found in a strain containing active PrB. We have purified this larger form of PrA and determined that it bears 7 additional amino acids at its NH2 terminus. It has become apparent from all the studies performed on the maturation pathway of the vacuolar hydrolases that there is a great deal of redundancy built into the system. |
| Databáze: | OpenAIRE |
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