Kohl, N. E., Diehl, R. E., Schaber, M. D., Rands, E., Soderman, D. D., He, B., Moores, S. L., Pompliano, D. L., Ferro-Novick, S., Powers, S. (October 1991) Structural homology among mammalian and Saccharomyces cerevisiae isoprenyl-protein transferases. Journal of Biological Chemistry, 266 (28). pp. 18884-8. ISSN 0021-9258
Abstract
Farnesyl-protein transferase (FTase) purified from rat or bovine brain is an alpha/beta heterodimer, comprised of subunits having relative molecular masses of approximately 47 (alpha) and 45 kDa (beta). In the yeast Saccharomyces cerevisiae, two unlinked genes, RAM1/DPR1 (RAM1) and RAM2, are required for FTase activity. To explore the relationship between the mammalian and yeast enzymes, we initiated cloning and immunological analyses. cDNA clones encoding the 329-amino acid COOH-terminal domain of bovine FTase alpha-subunit were isolated. Comparison of the amino acid sequences deduced from the alpha-subunit cDNA and the RAM2 gene revealed 30% identity and 58% similarity, suggesting that the RAM2 gene product encodes a subunit for the yeast FTase analogous to the bovine FTase alpha-subunit. Antisera raised against the RAM1 gene product reacted specifically with the beta-subunit of bovine FTase, suggesting that the RAM1 gene product is analogous to the bovine FTase beta-subunit. Whereas a ram1 mutation specifically inhibits FTase, mutations in the CDC43 and BET2 genes, both of which are homologous to RAM1, specifically inhibit geranylgeranyl-protein transferase (GGTase) type I and GGTase-II, respectively. In contrast, a ram2 mutation impairs both FTase and GGTase-I, but has little effect on GGTase-II. Antisera that specifically recognized the bovine FTase alpha-subunit precipitated both bovine FTase and GGTase-I activity, but not GGTase-II activity. Together, these results indicate that for both yeast and mammalian cells, FTase, GGTase-I, and GGTase-II are comprised of different but homologous beta-subunits and that the alpha-subunits of FTase and GGTase-I share common features not shared by GGTase-II.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | *Alkyl and Aryl Transferases Amino Acid Sequence Animals Base Sequence Cattle Cloning, Molecular Dna Immunoblotting Mammals Molecular Sequence Data Precipitin Tests Saccharomyces cerevisiae/*enzymology Sequence Alignment Transferases/*chemistry/genetics/metabolism |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification organism description > yeast |
| CSHL Authors: | |
| Communities: | CSHL labs > Powers lab |
| Depositing User: | Matt Covey |
| Date: | 5 October 1991 |
| Date Deposited: | 25 Feb 2014 21:03 |
| Last Modified: | 25 Feb 2014 21:03 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/29540 |
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