Abstract
A small number of nucleotides are released from highly purified reovirus double-stranded RNA by ribonuclease T 1 in the presence of 0.3 m NaCl. These nucleotides include ppGp, which is quantitatively released from the RNA, and lesser amounts of ApUpGp, Gp, and ApGp. The same products are released from each of the three size classes of double-stranded RNA segments. In experiments involving specific labeling of termini, the only demonstrable sites of hydrolysis were at the 5′ termini of the minus strands. The limited extent of ribonuclease T 1 hydrolysis and localization of its action at the 5′ termini of the minus strands are compatible with a perfect duplex structure for the double-stranded RNA segments wherein the secondary structure of the termini is less stable than that of internal regions.
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