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Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: Carboxyl methyltransferase
Author(s) -
Ashby Matthew N.,
Errada Patrick R.,
Boyartchuk Victor L.,
Rine Jasper
Publication year - 1993
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320090810
Subject(s) - biology , gene , genetics , methyltransferase , dna methyltransferase , peptide sequence , genomic dna , mutant , microbiology and biotechnology , biochemistry , methylation
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 Bam HI 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.