ArticleMolecular and cellular biology1990
Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 115 citations in OpenAlex.
- Photoswitchable Isoprenoid Lipids Enable Optical Control of Peptide Lipidation.ACS chemical biology · 2022Article
- Epimerization-free access to C-terminal cysteine peptide acids, carboxamides, secondary amides, and estersChemical science · 2018Article
- Activation of the Mating Pheromone Response Pathway ofMycobiology · 2018Article
- Isoprenyl carboxyl methyltransferase inhibitors: a brief review including recent patents.Amino acids · 2017Review
- a-Factor: a chemical biology tool for the study of protein prenylation.Current topics in peptide & protein research · 2017Article
- Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase.MedChemComm · 2016Article
- Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.Microbiology and molecular biology reviews : MMBR · 2012Review
- Inhibitors of protein geranylgeranyltransferase-I lead to prelamin A accumulation in cells by inhibiting ZMPSTE24.Journal of lipid research · 2012Article
- Amide-modified prenylcysteine based Icmt inhibitors: Structure-activity relationships, kinetic analysis and cellular characterization.Bioorganic & medicinal chemistry · 2012Article
- Probing the isoprenylcysteine carboxyl methyltransferase (Icmt) binding pocket: sulfonamide modified farnesyl cysteine (SMFC) analogs as Icmt inhibitors.Bioorganic & medicinal chemistry letters · 2011Article
- Functional oligomerization of the Saccharomyces cerevisiae isoprenylcysteine carboxyl methyltransferase, Ste14p.The Journal of biological chemistry · 2010Article
- Isoprenylcysteine methylation and demethylation regulate abscisic acid signaling in Arabidopsis.The Plant cell · 2008Article
- HIV-protease inhibitors block the enzymatic activity of purified Ste24p.Biochemical and biophysical research communications · 2008Article
- Synthesis of desthio prenylcysteine analogs: sulfur is important for biological activity.Bioorganic & medicinal chemistry letters · 2005Article
- The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: development of novel inhibitors.The Journal of biological chemistry · 2005Article
- Topological and mutational analysis of Saccharomyces cerevisiae Ste14p, founding member of the isoprenylcysteine carboxyl methyltransferase family.Molecular biology of the cell · 2001Article
- H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway.Molecular and cellular biology · 2000Article
- Solubilization and partial characterization of homogalacturonan-methyltransferase from microsomal membranes of suspension-cultured tobacco cells.Plant physiology · 1999Article
- Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Prenylcysteine alpha-carboxyl methyltransferase in suspension-cultured tobacco cellsPlant physiology · 1998Article
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2 authors at 1 institution in 1 country.
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Abstract
Membrane extracts of sterile Saccharomyces cerevisiae strains containing the a-specific ste14 mutation lack a farnesyl cysteine C-terminal carboxyl methyltransferase activity that is present in wild-type a and alpha cells. Other a-specific sterile strains with ste6 and ste16 mutations also have wild-type levels of the farnesyl cysteine carboxyl methyltransferase activity. This enzyme activity, detected by using a synthetic peptide sequence based on the C-terminus of a ras protein, may be responsible not only for the essential methylation of the farnesyl cysteine residue of a mating factor, but also for the methylation of yeast RAS1 and RAS2 proteins and possibly other polypeptides with similar C-terminal structures. We demonstrate that the farnesylation of the cysteine residue in the peptide is required for the methyltransferase activity, suggesting that methyl esterification follows the lipidation reaction in the cell. To show that the loss of methyltransferase activity is a direct result of the ste14 mutation, we transformed ste14 mutant cells with a plasmid complementing the mating defect of this strain and found that active enzyme was produced. Finally, we demonstrated that a similar transformation of cells possessing the wild-type STE14 gene resulted in sixfold overproduction of the enzyme. Although more complicated possibilities cannot be ruled out, these results suggest that STE14 is a candidate for the structural gene for a methyltransferase involved in the formation of isoprenylated cysteine alpha-methyl ester C-terminal structures.
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