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Gene Review

RAM1  -  protein farnesyltransferase

Saccharomyces cerevisiae S288c

Synonyms: CAAX farnesyltransferase subunit beta, D2412, DPR1, FTase-beta, FUS8, ...
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Disease relevance of RAM1

  • Extracts derived from an E. coli strain that coexpressed RAM1 and RAM2 efficiently farnesylated a-factor peptide and Ras protein substrates [1].
  • (i) The cloned SGP2 complements both the temperature-sensitive growth and the a-specific sterility of the dpr1 mutant and can be integrated into the chromosomal DPR1 locus [2].

High impact information on RAM1

  • Mutations in SUPH-STE16 prevent the membrane localization and maturation of RAS protein, as well as the fatty acid acylation of it and other membrane proteins [3].
  • We have identified a gene (SUPH) of S. cerevisiae that is required for both RAS function and mating by cells of a mating type. supH is allelic to ste16, a gene required for the production of the mating pheromone a-factor [3].
  • DNA sequence analysis has revealed that Bet2 is homologous to Dpr1 (Ram1), an essential component of a protein prenyltransferase that modifies Ras, enabling it to attach to membranes [4].
  • 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 [5].
  • Consistent with an a-specific defect, the fus5 and fus8 mutants produced less a-factor than the isogenic wild-type strain [6].

Biological context of RAM1

  • Therefore, we examined the relationship between farnesylation and proteolysis directly using extracts prepared from bacteria overexpressing the genes for the yeast FTase (RAM1 and RAM2) and synthetic CaaX box peptides [7].
  • RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins [1].
  • A series of plasmids for the expression of RAM1 and RAM2 in Escherichia coli was prepared and evaluated [8].
  • Strikingly, fus5 and fus8 were a specific; both mutations caused the mutant phenotype when present in the MATa parent but not in the MAT alpha parent [6].
  • We report the characterization of two cell fusion defective (Fus-) mutants, fus5 and fus8, isolated previously in our laboratory [6].

Anatomical context of RAM1


Associations of RAM1 with chemical compounds


Other interactions of RAM1

  • These results demonstrate that at least two genes, DPR1/RAM1 and RAM2, are required for the farnesyltransferase activity in yeast [12].
  • However, addition of yeast extracts from wild type, ram1, or ste14 mutants resulted in the removal of the -aaX residues from prenylated CaaX box peptides [7].
  • Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product [13].
  • However, inactivation of the prenyltransferase by disruption of DPR1 has only a minor effect on Ste18-dependent mating [14].
  • (i) In the dpr1 cells, the RAS2 proteins remain as precursors and accumulate in the cytoplasm [9].

Analytical, diagnostic and therapeutic context of RAM1

  • 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 [5].
  • The protein farnesyltransferase (PFT) beta-subunit gene of Saccharomyces cerevisiae, DPR1, was randomly mutagenized by PCR to construct a mutant DPR1 gene library on a high-copy plasmid [15].
  • 5. Reverse transcriptase-polymerase chain reaction, protein immuno-blots, and transient expression assays of green fluorescent protein fusion proteins show that GGT-IB is ubiquitously expressed in a number of tissues, and that expression levels and protein activity were not changed in mutant plants lacking FTase beta-subunit [16].


  1. RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins. He, B., Chen, P., Chen, S.Y., Vancura, K.L., Michaelis, S., Powers, S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  2. Role of SGP2, a suppressor of a gpa1 mutation, in the mating-factor signaling pathway of Saccharomyces cerevisiae. Nakayama, N., Arai, K., Matsumoto, K. Mol. Cell. Biol. (1988) [Pubmed]
  3. RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor. Powers, S., Michaelis, S., Broek, D., Santa Anna, S., Field, J., Herskowitz, I., Wigler, M. Cell (1986) [Pubmed]
  4. Dependence of Ypt1 and Sec4 membrane attachment on Bet2. Rossi, G., Yu, J.A., Newman, A.P., Ferro-Novick, S. Nature (1991) [Pubmed]
  5. Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the ras protein. Schafer, W.R., Trueblood, C.E., Yang, C.C., Mayer, M.P., Rosenberg, S., Poulter, C.D., Kim, S.H., Rine, J. Science (1990) [Pubmed]
  6. Cell fusion during yeast mating requires high levels of a-factor mating pheromone. Brizzio, V., Gammie, A.E., Nijbroek, G., Michaelis, S., Rose, M.D. J. Cell Biol. (1996) [Pubmed]
  7. Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modification pathway. Farh, L., Mitchell, D.A., Deschenes, R.J. Arch. Biochem. Biophys. (1995) [Pubmed]
  8. Protein farnesyltransferase: production in Escherichia coli and immunoaffinity purification of the heterodimer from Saccharomyces cerevisiae. Mayer, M.P., Prestwich, G.D., Dolence, J.M., Bond, P.D., Wu, H.Y., Poulter, C.D. Gene (1993) [Pubmed]
  9. A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps. Fujiyama, A., Matsumoto, K., Tamanoi, F. EMBO J. (1987) [Pubmed]
  10. Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae. Hrycyna, C.A., Clarke, S. Mol. Cell. Biol. (1990) [Pubmed]
  11. Amino acid substitutions that convert the protein substrate specificity of farnesyltransferase to that of geranylgeranyltransferase type I. Del Villar, K., Mitsuzawa, H., Yang, W., Sattler, I., Tamanoi, F. J. Biol. Chem. (1997) [Pubmed]
  12. Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins. Goodman, L.E., Judd, S.R., Farnsworth, C.C., Powers, S., Gelb, M.H., Glomset, J.A., Tamanoi, F. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  13. Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product. Finegold, A.A., Johnson, D.I., Farnsworth, C.C., Gelb, M.H., Judd, S.R., Glomset, J.A., Tamanoi, F. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  14. Site-directed mutations altering the CAAX box of Ste18, the yeast pheromone-response pathway G gamma subunit. Whiteway, M.S., Thomas, D.Y. Genetics (1994) [Pubmed]
  15. Mutant farnesyltransferase beta subunit of Saccharomyces cerevisiae that can substitute for geranylgeranyltransferase type I beta subunit. Mitsuzawa, H., Esson, K., Tamanoi, F. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  16. Efficient prenylation by a plant geranylgeranyltransferase-I requires a functional CaaL box motif and a proximal polybasic domain. Caldelari, D., Sternberg, H., Rodríguez-Concepción, M., Gruissem, W., Yalovsky, S. Plant Physiol. (2001) [Pubmed]
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