特定结构修饰对大肠杆菌精氨酸tRNA生物活性的影响。
The effect of specific structural modification on the biological activity of E. coli arginine tRNA.
作者信息
Kruse T A, Clark B F
出版信息
Nucleic Acids Res. 1978 Mar;5(3):879-92. doi: 10.1093/nar/5.3.879.
Abstract
Escherichia coli arginine tRNA1 has been modified at position s2C32 with iodoacetamide and a spin labelled derivative. The small effects on the charging ability of tRNA by the modifiications suggest that the synthetase does not bind to the tRNA in this region of the anticodon loop before the anticodon. A ternary complex of elongation factor Tu, GTP and the modified Arg-tRNA, can be formed allowing future studies of enzymatic binding to the ribosome. Using the triplet binding assay the native Arg-tRNA1 decodes all 4 codons beginning with CG. The modified Arg-tRNA1 has a restricted decoding but the decoding pattern is still unusual according to the Wobble Hypothesis.
摘要
大肠杆菌精氨酸tRNA1在第32位的s2C处用碘乙酰胺和自旋标记衍生物进行了修饰。这些修饰对tRNA充电能力的影响较小，这表明合成酶在反密码子之前的反密码子环的这个区域不会与tRNA结合。可以形成延伸因子Tu、GTP和修饰后的精氨酸-tRNA的三元复合物，以便未来研究酶与核糖体的结合。使用三联体结合试验，天然的精氨酸-tRNA1能解码所有以CG开头的4个密码子。修饰后的精氨酸-tRNA1的解码受到限制，但根据摆动假说，其解码模式仍然不寻常。
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