Conversion of the guanine nucleotide binding sites of ras protein resulting in the reduction of base specificity |
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| Authors: | Miura, Kazunobu Kamiya, Hiroyuki Kubota, Sachie Ikehara, Morio Nishimura, Susumu Ohtsuka, Eiko |
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| Affiliation: | Faculty of Pharmaceutical Sciences, Hokkaido University Sapporo 060 1Protein Engineering Research Institute Kodenmacho, Nihonbashi, Chuo-ku, Tokyo 103 2National Cancer Research Institute Tsukiji, Chuo-ku, Tokyo 105, Japan |
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| Abstract: | A gene coding for the novel ras protein, p21x, in which thedomains of guanine binding and phosphate binding were exchanged,was constructed and expressed in Escherichia coli. The geneproduct, p21x, showed GTP binding activity, but no GPTase activity.In addition, p21x revealed binding activity toward ATP and CTP.In a competitive binding assay, [3H]GTP binding to p21x wasinhibited in the presence of ATP, CTP and UTP, ITP as well asGDP, GTP and dGTP. |
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| Keywords: | c-Ha-ras gene/ domain-exchange mutation/ guanine nucleotide binding activity/ ATP and CTP binding activity |
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