Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical α and β subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The β subunit, which is known as FTβ, CAAX farnesyltransferase subunit β, or Ras proteins prenyltransferase subunit β, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The α subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.
