The Ras is a membrane protein, which is synthesized in the cytoplasm, but it binds to the membrane so as to interact with the receptor-ligand-signal protein complex. It is the class of signal protein, which functions like G-proteins.
Farnesyl transferase is an enzyme, which catalyses the attachment of a long hydrophobic chain to the Ras protein in the presence of certain cofactors like magnesium, and iron though transferase is a zinc metalloenzyme. The attachment of long hydrophobic chain anchors the Ras chain after the attachment of that chain by the farnesyl transferase.
This initiates the activation or deactivation of Ras protein that could be caused by binding of GTP (guanosine triphosphate) or GDP (guanosine diphosphate) respectively. If the enzyme farnesyl transferase is inhibited, then it would have its reverse effect as the enzyme would not be able to cause the attachment of a long hydrophobic farnesyl chain to the Ras protein.
This, in turn, would prevent the anchoring of the Ras protein towards the cell membrane. Hence, the GTP and GDP would not bind significantly to the protein. Since the binding of GTP or GDP can only activate or deactivate the Ras protein, which can further initiate a cascade of reactions for regulation of transcription of genes. Thus, the inhibition of the enzyme in either way would affect the transcription of the genes.