作者: Y Matsui , A Kikuchi , J Kondo , T Hishida , Y Teranishi
DOI: 10.1016/S0021-9258(18)37922-5
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摘要: We have purified a novel GTP-binding protein (G protein) with Mr of about 24,000 to homogeneity from bovine brain membranes (Kikuchi, A., Yamashita, T., Kawata, M., Yamamoto, K., Ikeda, Tanimoto, and Takai, Y. (1988) J. Biol. Chem. 263, 2897-2904). In the present studies, we isolated sequenced cDNA this G library using oligonucleotide probes designed partial amino acid sequences. The has an open reading frame encoding 220 acids calculated 24,954. This is designated as smg-25A (smg p25A). sequence deduced contains consensus sequences GTPase domains. smg p25A shares 28 44% homology ras ypt1 proteins, respectively. addition cDNA, two other homologous cDNAs proteins 219 227 values 24,766 25,975, These are smg-25B smg-25C p25B p25C), three smg-25 highly one another in overall except for C-terminal 32 acids. Moreover, p25s sequence, Cys-X-Cys, which different known Cys-X-X-X Cys-Cys, results together biochemical properties described previously indicate that constitute family.