Nonidentical subunits of p21H-ras farnesyltransferase: Peptide binding and farnesyl pyrophosphate carrier functions

Yuval Reiss, Miguel C. Seabra, Scott A. Armstrong, Clive A. Slaughter, Joseph L. Goldstein, Michael S. Brown

Research output: Contribution to journalArticlepeer-review

172 Scopus citations

Abstract

The protein farnesyltransferase purified from rat brain contains two nonidentical subunits, α and β. The holoenzyme forms a stable complex with [3H]farnesyl pyrophosphate (FPP) that can be isolated by gel filtration. The [3H]FPP is not covalently bound to the enzyme; it is released unaltered when the enzyme is denatured. When incubated with an acceptor such as p21H-ras, the complex transfers [3H]farnesyl from the bound [3H]FPP to the ras protein. This transfer is not sensitive to dilution by unbound FPP, suggesting that the [3H]FPP is bound at a site that leads to direct transfer to the p21H-ras acceptor. Cross-linking studies show that the p21H-ras binds to the lower molecular weight subunit (β-subunit), raising the possibility that the [3H]FPP binds to the α-subunit. If this suggestion can be confirmed, it would invoke a reaction mechanism in which the α-subunit acts as a prenyl pyrophosphate carrier that delivers FPP to p21H-ras which is bound to the β-subunit.

Original languageEnglish (US)
Pages (from-to)10672-10677
Number of pages6
JournalJournal of Biological Chemistry
Volume266
Issue number16
StatePublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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