Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: carboxyl methyltransferase.
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 profile of the methyltransferase reveals the presence of at least five potential transmembrane domains. In comparisons of the C-terminal methyltransferase amino acid sequence with those in the PIR and Swiss protein databases, no significantly similar sequences were found nor were conserved regions from other methyltransferases present.
Ashby
M N
MN
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Errada
P R
PR
Boyartchuk
V L
VL
Rine
J
J
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D005800:Genes, Fungal / Q000235:genetics*; D005816:Genetic Complementation Test; D015698:Genomic Library; D008780:Methyltransferases / Q000235:genetics; D008969:Molecular Sequence Data; D011496:Protein Methyltransferases / Q000235:genetics*; D017368:Protein Prenylation / Q000235:genetics*; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)
D008780:Methyltransferases; D011496:Protein Methyltransferases; C056501:protein-S-isoprenylcysteine O-methyltransferase; C058693:Dam methyltransferase; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)