Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides.
Cell
; 62(1): 81-8, 1990 Jul 13.
Article
em En
| MEDLINE
| ID: mdl-2194674
ABSTRACT
We report the identification, purification, and characterization of a farnesylprotein 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.
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Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Transferases
/
Encéfalo
/
Proteínas Proto-Oncogênicas
/
Alquil e Aril Transferases
Limite:
Animals
Idioma:
En
Ano de publicação:
1990
Tipo de documento:
Article