ABSTRACT
The action of the guanylyl-preferring RNase from Bacillus intermedius (binase) on a mixture of oligoadenylates with randomly distributed 2'-5' and 3'-5' internucleotide bonds [(A2'/3'p)n] under conditions sufficient for complete hydrolysis of poly(A) results in a mixture containing a single circular oligoadenylate and two series of linear oligoadenylates ending in cyclic 2',3'-phosphate. Individual compounds formed upon digestion of (A2'/3'p)n with binase have been isolated. Their structure was determined on the basis of their chemical and enzymatic conversions and confirmed by 1H-, 13C- and 31P-NMR spectra. According to these data, the circular triadenylate contains one 2'-5' and two 3'-5' internucleotide bonds, linear oligoadenylates of one series contain exclusively 2'-5' internucleotide bonds [(A2'p)nA > p], while each compound of the other series contains a single 3'-5' internucleotide bond connecting the 5'-ultimate nucleotide residue with the penultimate one [A3'p(A2'p)n-1A > p]. The incubation of compounds of the former series A3' p(A2'p)n > p at pH 1.0 and the subsequent action of phosphatase results in successive formation of compounds of two other new series: A3'p(A2'p)nA2'(3')p and A3'p(A2'p)nA.
