Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides

Yuval Reiss, Joseph L. Goldstein, Miguel C. Seabra, Patrick J. Casey, Michael S. Brown

Research output: Contribution to journalArticlepeer-review

702 Scopus citations


We report the identification, purification, and characterization of a farnesyl:protein transferase that transfers the farnesyl moiety from farnesyl pyrophosphate to a cysteine in p21ras proteins. The enzyme was purified ∼60,000-fold from rat brain cytosol through use of a chromatography step based on the enzyme's ability to bind to a hexapeptide containing the consensus sequence (Cys-AAX) for farnesylation. The purified enzyme migrated on gel filtration chromatography with an apparent molecular weight of 70,000-100,000. High resolution SDS-polyacrylamide gels showed two closely spaced ∼50 kd protein bands in the final preparation. The enzyme was inhibited competitively by peptides as short as 4 residues that contained the Cys-AAX motif. These peptides acted as alternative substrates that competed with p21H-ras for farnesylation. Effective peptides included the COOH-terminal sequences of all known p21ras proteins as well as those of lamin A and B.

Original languageEnglish (US)
Pages (from-to)81-88
Number of pages8
Issue number1
StatePublished - Jul 13 1990

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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