TRANSFER RNA, III. RECONSTITUTION OF ALANINE ACCEPTOR ACTIVITY FROM FRAGMENTS PRODUCED BY SPECIFIC CLEAVAGE OF tRNAAlaII AT ITS ANTICODON*†

AUTOR(ES)

Imura, Nobumasa

RESUMO

This report describes experiments showing that tRNAAlaII can be cleaved specifically at the G residue of its anticodon to give “half” molecules in high yield. Neither of these fragments has alanine-acceptor activity, but this activity can be reconstituted by mixing the fragments in the presence of Mg+2. In dilute salt, on the other hand, the active complex dissociates spontaneously at 25° into the two fragments. Thus, both “halves” of tRNAAlaII are necessary for acceptor activity and, in the presence of Mg+2, combination of these fragments to give an active duplex is thermodynamically favorable.

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