An NTP-Binding Protein That Cross-Reacts with a Ras-Specific Antibody in the Mycelia of Neurospora crassa : ENVIRONMENTAL AND STRESS RESPONSES : PROTEINS, ENZYMES AND METABOLISM
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概要
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A Ras-related NTP-binding protein was partially purified from a membrane fraction derived from the mycelia of Neurospora crassa. [a-^<32>P]ATP and [a-^<32>P]GTP were incubated with membrane and soluble fractions which were then irradiated with UV light to induce crosslinking of tightly bound nucleotides. After SDS-polyacrylamide gel electrophoresis, blotting onto a nitrocellulose filter and autoradiography it was apparent that most of the proteins that bound [a-^<32>P]-GTP also bound [a-^<32>P]ATP. Pretreatment of the membrane fraction with Ras-specific antibody effectively blocked the binding of [a-^<32>P]ATP and [a-^<32>P]GTP to several ATP-GTP-binding proteins. The band of a protein with a molecular weight of 26 kDa on the SDS-polyacrylamide gel cross-reacted strongly with the Ras-specific antibody. The protein was extracted from the gel and further purified by repeated gel electrophoresis. The purified protein bound [a-^<32>P]ATP, [a-^<32>P]-GTP, [a-^<32>P]CTP and [a-^<32>P]UTP at 1.6×10^<-7> M and was autophosphorylated in the presence of [ν-^<32>P]ATP and [ν-^<32>P]GTP at 1.7×10^<-7> M. Pretreatment of the protein with Ras-specific antibody partially blocked the autophosphorylation in the presence of these nucleotides. The binding of [a-^<32>P]ATP to the NTP-binding protein was blocked by addition of ATP at 10^<-4>-10^<-3> M. ATP at a concentration of 10^<-4> M prevented the binding of [a-^<32>P]GTP to a greater extent than did GTP at the same concentration. Binding of [a-^<32>P]CTP and [a-^<32>P]UTP to the protein was also observed.
- 日本植物生理学会の論文
著者
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HASUNUMA Kohji
Yokohama City Univ. , Kihara Inst. Biol. Res.
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Nishikawa Kazuko
Yokohama City University, Kihara Institute for Biological Research
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Nishikawa Kazuko
Dept. Applied Biol. Chem. Univ. Osaka. Pref.
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