TY - JOUR
T1 - A geranylgeranyltransferase for rhoA p21 distinct from the farnesyltransferase for ras p21A
AU - Yoshida, Yasuhisa
AU - Kawata, Masahito
AU - Katayama, Masaya
AU - Horiuchi, Hisanori
AU - Kita, Yasuhiro
AU - Takai, Yoshimi
N1 - Funding Information:
'This investigation was supported by grants-in-aid for Scientific Research and Cancer Research from the Ministry Education, Science, and Culture, Japan (1990), a grant-in-aid for Abnormalities in Hormone Receptor Mechanisms from the Ministry of Health and Welfare, Japan (1990), and by grants from the Human Frontier Science Program (1990), the Yamanouchi Foundation for Re-search on Metabolic Disease (1990), and the Research Program on Cell Calcium Signal in the Cardiovascular System (1990). 2To whom correspondence should be addressed. Abbreviations used are: G proteins, GTP-binding proteins; FT, farnesyltransferase; GGT, geranylgeranyltransferase; E. coli, Escherichia coli; rhoA p21-CAAX, rhoA p21 having the C-terminal CAAX motif; rhoA p21-C, rhoA ~21 lacking the AAX portion; c-Ha-ras p21-CAAX, c-Ha-ras p21 having the C-terminal CAAX motif; GGpp, all-trans-geranylgeranyl pyrophosphate; Fpp, all-trans-farnesyl pyro-phosphate; DTT, dithiothreitol; SDS, sodium dodecyl sulfate; TCA, trichloroacetic acid; GG, all-trans-geranylgeranyl; HPLC, high per-formance liquid chromatography; API, Achromobacter protease I; Mr, relative molecular mass.
PY - 1991/3/15
Y1 - 1991/3/15
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(91)91625-M
DO - 10.1016/0006-291X(91)91625-M
M3 - Article
C2 - 1902099
AN - SCOPUS:0025745256
VL - 175
SP - 720
EP - 728
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -