Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: Carboxyl methyltransferase

@article{Ashby1993IsolationAD,
  title={Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: Carboxyl methyltransferase},
  author={Matthew N. Ashby and P R Errada and Victor Boyartchuk and Jasper Rine},
  journal={Yeast},
  year={1993},
  volume={9}
}
We isolated a mutant defective in C‐terminal farnesyl cysteine:carboxyl methyltransferase activity from a screen for mutations causing a‐specific sterility. A genomic fragment was cloned from a yeast multi‐copy library that restored mating. Both the cloned gene and the sterile mutation were allelic to the STE14 gene. A ste14‐complementing 2·17 kb BamHI fragment subclone was sequenced and found to encode a 239 amino acid protein with a molecular weight of 27,887 Daltons. The hydrophobicity… Expand
Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export.
TLDR
The nucleotide sequence of STE14 is reported, which indicates that STE14 encodes a protein of 239 amino acids, predicted to contain multiple membrane-spanning segments, thus providing insight into the substrate specificity of STE6 and supporting the hypothesis that carboxyl methylation can have a dramatic impact on protein-protein interactions. Expand
Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export
Eukaryotic proteins initially synthesized with a C-terminal CAAX motif (C is Cys, A is aliphatic, and X can be one of several amino acids) undergo a series of modifications involving isoprenylationExpand
Yeast STE14 methyltransferase, expressed as TrpE-STE14 fusion protein in Escherichia coli, for in vitro carboxylmethylation of prenylated polypeptides.
TLDR
This chapter discusses the preparation and assay of E. coli extracts containing C-terminal prenylcysteine methyltransferase activity, and the uses for the recombinant enzyme, including use of TrpE-STE14 methyl transferase in a coupled assay to identify proteolytic activities capable of removing the aaX residues from a CaaX-containing substrate. Expand
Genes encoding farnesyl cysteine carboxyl methyltransferase in Schizosaccharomyces pombe and Xenopus laevis
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The isolation of a vertebrate gene encoding farnesyl cysteine carboxyl methyltransferase opens the way to in-depth studies of the role of methylation in a large body of proteins, including Ras superfamily proteins. Expand
Plant farnesyltransferase can restore yeast Ras signaling and mating
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Yeast and plant FTases shared similar in vivo and in vitro substrate specificities, demonstrating that this enzymatic modification of proteins with intermediates from the isoprenoid biosynthesis pathway is conserved in evolutionarily divergent eukaryotes. Expand
Topological and mutational analysis of Saccharomyces cerevisiae Ste14p, founding member of the isoprenylcysteine carboxyl methyltransferase family.
TLDR
A novel tripartite consensus motif in the C-terminal region of Ste14p is identified, which is similar among all ICMT family members, two phospholipid methyltransferases, several ergosterol biosynthetic enzymes, and a group of bacterial open reading frames of unknown function. Expand
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Methyltransferase activity was detected in the membrane fraction from Sf9 cells infected with the recombinant baculovirus using N -acetyl- S -farnesylcysteine (AFC) and S -adenosyl[ methyl -(3)H]methionine ([(3]H]AdoMet) as substrates, suggesting that T. brucei PPMT acts on farnesylated proteins in the cell. Expand
Fungal lipopeptide mating pheromones: a model system for the study of protein prenylation.
In a variety of fungal species, mating between haploid cells is initiated by the action of peptide pheromones. The identification and characterization of several fungal pheromones has revealed thatExpand
Fungal lipopeptide mating pheromones: a model system for the study of protein prenylation
In a variety of fungal species, mating between haploid cells is initiated by the action of peptide pheromones. The identification and characterization of several fungal pheromones has revealed thatExpand
Restricted Substrate Specificity for the Geranylgeranyltransferase-I Enzyme in Cryptococcus neoformans: Implications for Virulence
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It is found that Ggtase-I function is required for full membrane localization of Rho10 and the two Cdc42 paralogs (Cdc42 and Cdc420). Expand
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TLDR
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