| Autor: |
Schafer WR; Department of Molecular and Cell Biology, University of California, Berkeley 94720., Trueblood CE, Yang CC, Mayer MP, Rosenberg S, Poulter CD, Kim SH, Rine J |
| Jazyk: |
angličtina |
| Zdroj: |
Science (New York, N.Y.) [Science] 1990 Sep 07; Vol. 249 (4973), pp. 1133-9. |
| DOI: |
10.1126/science.2204115 |
| Abstrakt: |
The post-translational processing of the yeast a-mating pheromone precursor, Ras proteins, nuclear lamins, and some subunits of trimeric G proteins requires a set of complex modifications at their carboxyl termini. This processing includes three steps: prenylation of a cysteine residue, proteolytic processing, and carboxymethylation. In the yeast Saccharomyces cerevisiae, the product of the DPR1-RAM1 gene participates in this type of processing. Through the use of an in vitro assay with peptide substrates modeled after a presumptive a-mating pheromone precursor, it was discovered that mutations in DPR1-RAM1 cause a defect in the prenylation reaction. It was further shown that DPR1-RAM1 encodes an essential and limiting component of a protein prenyltransferase. These studies also implied a fixed order of the three processing steps shared by prenylated proteins: prenylation, proteolysis, then carboxymethylation. Because the yeast protein prenyltransferase could also prenylate human H-ras p21 precursor, the human DPR1-RAM1 analogue may be a useful target for anticancer chemotherapy. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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