Substrate specificity of the exonuclease activity that degrades H4 histone mRNA.
We have investigated the substrate specificity of an exonuclease that degrades human H4 histone mRNA, using synthetic RNA templates incubated in a cell-free mRNA decay system (Ross, J., and Kobs, G. (1986) J. Mol. Biol. 188, 579-593). Five RNAs that lacked poly(A), including histone, were degraded rapidly in vitro. Polyadenylated histone mRNA was degraded at least 10-fold more slowly than unmodified histone mRNA. Double-stranded RNA and DNA were very stable. Single-stranded DNA was degraded approximately 20-fold more slowly than single-stranded, non-polyadenylated RNA, and RNA with a 3' phosphoryl group was degraded more slowly than RNA with a 3'-hydroxyl group. Uncapped RNAs were degraded rapidly in the unfractionated system but were stable in reactions containing a ribosomal high salt wash extract. Therefore, the exonuclease activity released from ribosomes by high salt extraction was separated from the enzyme(s) that degraded uncapped RNAs.
D004247:DNA / Q000378:metabolism; D004262:DNA Restriction Enzymes / Q000378:metabolism; D005092:Exonucleases / Q000378:metabolism*; D005914:Globins / Q000235:genetics; D006657:Histones / Q000235:genetics*; D006801:Humans; D010957:Plasmids; D012333:RNA, Messenger / Q000378:metabolism*; D013379:Substrate Specificity
D006657:Histones; D012333:RNA, Messenger; D005914:Globins; D004247:DNA; D005092:Exonucleases; D004262:DNA Restriction Enzymes