Abstract |
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.
|
Authors | M N Ashby, P R Errada, V L Boyartchuk, J Rine |
Journal | Yeast (Chichester, England)
(Yeast)
Vol. 9
Issue 8
Pg. 907-13
(Aug 1993)
ISSN: 0749-503X [Print] England |
PMID | 8212897
(Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
|
Chemical References |
- Methyltransferases
- Protein Methyltransferases
- protein-S-isoprenylcysteine O-methyltransferase
- Dam methyltransferase
- Site-Specific DNA-Methyltransferase (Adenine-Specific)
|
Topics |
- Amino Acid Sequence
- Base Sequence
- Cloning, Molecular
- Genes, Fungal
(genetics)
- Genetic Complementation Test
- Genomic Library
- Methyltransferases
(genetics)
- Molecular Sequence Data
- Protein Methyltransferases
(genetics)
- Protein Prenylation
(genetics)
- Restriction Mapping
- Saccharomyces cerevisiae
(enzymology, genetics)
- Sequence Analysis, DNA
- Sequence Homology, Amino Acid
- Site-Specific DNA-Methyltransferase (Adenine-Specific)
|