| Autor: |
C A, Woolford, J A, Noble, J D, Garman, M F, Tam, M A, Innis, E W, Jones |
| Rok vydání: |
1993 |
| Předmět: |
|
| Zdroj: |
The Journal of biological chemistry. 268(12) |
| ISSN: |
0021-9258 |
| 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 |
| Externí odkaz: |
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