Abstract
Protein farnesyltransferase is a heterodimeric enzyme that attaches a farnesyl group to cysteine in ras proteins and other membrane-associated proteins. The β subunit contains the recognition site for the peptide substrates, but is inactive in the absence of the α subunit. A cloned cDNA for the rat β subunit predicts a protein of 437 amino acids whose mRNA is present in many tissues. Transfection of the β subunit cDNA produced farnesyltransferase activity in human kidney cells, but only when it was transfected together with a cDNA encoding part of the α subunit. Each of the subunits appeared to be unstable in the transfected cells unless the other subunit was present. The rat β subunit shows 37% sequence identity with the protein encoded by the yeast DPR1/RAM1 gene, indicating that DPR1/RAM1 is the yeast counterpart of the peptide-binding subunit of the mammalian farnesyltransferase.
| Original language | English |
|---|---|
| Pages (from-to) | 327-334 |
| Number of pages | 8 |
| Journal | Cell |
| Volume | 66 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 26 1991 |
Bibliographical note
Funding Information:We thankourcolleaguesYuva1 Reissand MiguelSeabrafor invaluable discussions. Jeff Cormier, Gloria Brunschede, and Debbie Noble provided excellent technical assistance. This research was supported by grants from the National Institutes of Health (HL 20948) the Lucille p. Markey Charitable Trust, and the Perot Familv Foundation.
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology