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Nucleic Acids Research, 1979, Vol. 6, No. 3 899-914
© 1979

Articles

chemical modification study of aminoacyl-tRNA conformation

Kazuo Negishi1, Susumu Nishimura2, Fumio Harada2 and Hikoya Hayatsu1

1Faculty of Pharamaceutical Sciences, University of Tokyo Bunkyo-ku, Tokyo 2National Cancer Center Research Institute Tsukiji, Chuo-ku, Tokyo, Japan

Received December 20, 1978. Chemical reactivity of cytosines in 32P-labeled E. coli tRNAFormula, 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 T{psi}C(G) sequence could become exposed in later steps of protein synthesis in order to achieve the binding of aminoacyl tRNA to ribosomes.


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