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chemical modification study of aminoacyl-tRNA conformation

机译：氨基酰基-TRNA构象的化学改性研究

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Chemical reactivity of cytosines in 32P-labeled E. coli tRNA, E. coli tRNAPhe and yeast tRNAPhe before and after aminoacylation was examined by use of a cytosine-apecific reagent, semicarbazide-bisulfite mixture. In all the three tRNA species examined, the cytosine residues that were susceptible to the modification were the same in the aminoacylated tRNA and the unacylated tRNA. Only a limited number of the cytosine residues were modifiable: those that occur in the anticodon, the 3′-CCA terminus, the D-loop, and the extra loop. The sites accessible by the reagent are in good agreement with the general three-dimensional structure of tRNA proposed in literature. These results indicate that the gross conformation of these tRNAs does not change on aminoacylation, and consequently favor the view that the TψC(G) sequence could become exposed in later steps of protein synthesis in order to achieve the binding of aminoacyl tRNA to ribosomes.
机译：检查氨基酰化之前和之后，在氨基乙基化之前和之后和在氨基酰化之前和之后的氨基酰化之前和酵母TrNA phe phe phe phe phe phe phe中的化学反应性通过使用胞嘧啶至透氧试剂，氨基脲 - 亚硫酸氢盐混合物。在所检查的所有三种TRNA种类中，氨基酰化的TRNA和未解剖的TRNA中易受该修饰的胞嘧啶残基相同。只有有限数量的胞嘧啶残留是可修改的：那些在抗oryon，3'-CCA末端，D圈和额外环中发生的那些。试剂可访问的位点与文献中提出的三维结构一致。这些结果表明，这些TrNA的总构象不会改变氨基化酶，因此有利于T 1C（G）序列在蛋白质合成的后续步骤中暴露，以实现氨基酰基TRNA与核糖瘤的结合。

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