Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides.
Journal Article (Journal Article)
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 approximately 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 approximately 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.
Full Text
Duke Authors
Cited Authors
- Reiss, Y; Goldstein, JL; Seabra, MC; Casey, PJ; Brown, MS
Published Date
- July 13, 1990
Published In
Volume / Issue
- 62 / 1
Start / End Page
- 81 - 88
PubMed ID
- 2194674
International Standard Serial Number (ISSN)
- 0092-8674
Digital Object Identifier (DOI)
- 10.1016/0092-8674(90)90242-7
Language
- eng
Conference Location
- United States