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

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

研究成果: Article査読

54 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)720-728
ページ数9
ジャーナルBiochemical and biophysical research communications
175
2
DOI
出版ステータスPublished - 1991 3 15
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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