A geranylgeranyltransferase for rhoA p21 distinct from the farnesyltransferase for ras p21A

Yasuhisa Yoshida, Masahito Kawata, Masaya Katayama, Hisanori Horiuchi, Yasuhiro Kita, Yoshimi Takai

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)

Abstract

We have clarified that rhoA p21 purified from bovine aortic smooth muscle is geranylgeranylated at the cysteine residue in the C-terminal CAAX motif (A is an aliphatic amino acid and X is any amino acid). In this paper, a geranylgeranyltransferase for rhoA p21 (rhoA p21 GGT) was partially purified from bovine brain cytosol. This enzyme transferred a geranylgeranyl moiety from geranylgeranyl pyrophosphate to rhoA p21 having the CAAX motif (rhoA p21-CAAX) but not to rhoA p21 lacking the AAX portion. rhoA p21 GGT was separated from the previously reported farnesyltransferase for ras p21s (ras p21 FT) by column chromatographies and did not geranylgeranylate or farnesylate c-Ha-ras p21-CAAX. ras p21 FT did not geranylgeranylate or farnesylate rhoA p21-CAAX. These results indicate that rhoA p21 GGT distinct from ras p21 FT is present in bovine brain cytosol.

Original languageEnglish
Pages (from-to)720-728
Number of pages9
JournalBiochemical and biophysical research communications
Volume175
Issue number2
DOIs
Publication statusPublished - 1991 Mar 15
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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