Abstract
Abstract The hydrolytic action of spleen exonuclease on serine transfer RNA has been investigated. It was found that two different mechanisms of attack obtain: (a) processive degradation and (b) random cleavage. These two different modes of action are determined by the presence or the absence of the terminal phosphate group at the 5' terminus of transfer RNA. The loss of several important biological activities of transfer RNA or aminoacyl transfer RNA, such as amino acid acceptor activity, AMP acceptor activity, polynucleotide-directed ribosomal binding, and incorporation of the amino acid moiety into growing polypeptide chains, were examined in detail as a function of the digestion by spleen exonuclease.
Highlights
The hydrolytic action of spleen exonuclease on serine transfer RNA has been investigated
That an intact tRNA molecule would be completely resistant to this enzyme, whereas the enzyme should be able to hydrolyze tRNA after dephosphorylation
It should be noted that the loss of acceptor activity upon spleen exonuclease digestion follows a very different kinetic course from that observed with snake venom exonuclease
Summary
The hydrolytic action of spleen exonuclease on serine transfer RNA has been investigated. It was found that two different mechanismsof attack obtain: (a) processive degradation and (b) random cleavage. These two diiferent modes of action are determined by the presence or the absence of the terminal phosphategroup at the 5’ terminus of transfer. It becameof interestto study the mechanismof attack of spleenexonucleasoen tRNA andto examinein moredetail the effectsof gradeddigestionwith this enzymeon the ability of tRNA to participate in a numberof biologicalor enzymatic reactions. The resultsof thesestudiesare described in this communication. The loss of several important biological activities of transfer RNA or aminoacyl transfer RNA, such as amino acid acceptor activity, AMP acceptor activity, polynucleotidedirected ribosomal binding, and incorporation of the amino acid moiety into growing polypeptide chains, were examined in detail asa function of the digestionby spleenexonuclease
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