| ARGINYL-tRNA SYNTHETASE FROM Escherichia coli AFFINITY LABELING WITH 3''''-OXIDIZED tRNA~(Arg) |
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| 引用本文： | 程晓东,林胜祥,施建平,王应睐. ARGINYL-tRNA SYNTHETASE FROM Escherichia coli AFFINITY LABELING WITH 3''''-OXIDIZED tRNA~(Arg)[J]. 中国科学B辑(英文版), 1991, 0(3) |
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| 作者姓名： | 程晓东 林胜祥 施建平 王应睐 |
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| 作者单位： | Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica Shanghai 200031，PRC，Shanghai 200031，PRC，Shanghai 200031，PRC，Shanghai 200031，PRC |
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| 基金项目： | Project supported by the National Natural Science Foundation of China. |
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| 摘 要： | The covalent modification of E. coli arginyl-tRNA synthetase by the 2',3'-dialdehydederivative of tRNA~(Arg) (tRNA_(ox)~(Arg)) resulted in the complete inactivation of the ATP-PPi ex-change and aminoacylation activities of the enzyme. Sodium dodecyl sulfate polyacrylamide gelelectrophoresis of the ArgRS-tRNA_(ox)~(Arg) covalent complexes indicated that two bands simulta-neously appeared on the gel parallel with inactivation corresponding to different higher mo-lecular weights. This result was different from that of the other aminoacyl-tRNA synthetaselabeling systems as previously reported. Upon the ribonuclease treatment of the modifiedArgRS, less than 15% of both the initial ATP-PPi exchange and aminocylation activities wererecovered. During the whole process of labeling and RNase treatment, the two activities ofthe enzyme were closely associated.
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ARGINYL-tRNA SYNTHETASE FROM Escherichia coli AFFINITY LABELING WITH 3''''-OXIDIZED tRNA~(Arg) |
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| CHENG XIAO-DONG,LIN SHENG-XIANG,SHI JIAN-PING,WANG YING-LAI. ARGINYL-tRNA SYNTHETASE FROM Escherichia coli AFFINITY LABELING WITH 3''''-OXIDIZED tRNA~(Arg)[J]. Science in China(Chemistry), 1991, 0(3) |
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| Authors: | CHENG XIAO-DONG LIN SHENG-XIANG SHI JIAN-PING WANG YING-LAI |
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| Affiliation: | CHENG XIAO-DONG,LIN SHENG-XIANG,SHI JIAN-PING,WANG YING-LAI Shanghai Institute of Biochemistry,Academia Sinica,Shanghai 200031,PRC |
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| Abstract: | The covalent modification of E. coli arginyl-tRNA synthetase by the 2',3'-dialdehydederivative of tRNA~(Arg) (tRNA_(ox)~(Arg)) resulted in the complete inactivation of the ATP-PPi ex-change and aminoacylation activities of the enzyme. Sodium dodecyl sulfate polyacrylamide gelelectrophoresis of the ArgRS-tRNA_(ox)~(Arg) covalent complexes indicated that two bands simulta-neously appeared on the gel parallel with inactivation corresponding to different higher mo-lecular weights. This result was different from that of the other aminoacyl-tRNA synthetaselabeling systems as previously reported. Upon the ribonuclease treatment of the modifiedArgRS, less than 15% of both the initial ATP-PPi exchange and aminocylation activities wererecovered. During the whole process of labeling and RNase treatment, the two activities ofthe enzyme were closely associated. |
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| Keywords: | arginyl-tRNA synthetase arginine specific tRNA affinity labeling E. coli |
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