hide
Free keywords:
Nucleotide; Protein synthesis; Chain length; Degradation product; Sequence homology
Abstract:
Free cytoplasmic 40S mRNP particles from rat liver were treated with EDTA and separated into two populations of RNP particles with sedimentation maxima of 20S and 35S, respectively. A characteristic set of distinct scRNAs is found for 20S and 35S RNP particles.
The sequences of two of the most abundant scRNAs from 20S RNP particles with chain lengths of 104 (α1-RNA) and 124 (β1-RNA) nucleotides, respectively, are presented. α1-RNA shows a high sequence homology to the 3′-end of 18S rRNA. Since α1-RNA carries a cap, it cannot be a degradation product of 18S rRNA. The β1-RNA is strongly post-transcriptionally modified, but uncapped.
When the individual scRNAs of 20S and 35S RNP particles isolated from preparative polyacrylamide gels were assayed for their capability to inhibit in vitro protein synthesis, several potent translational inhibitory RNAs were detected. Particularly, the scRNAs of 147, 203 and 263 nucleotide length associated with the 35S RNP particles turned out to be strong inhibitors of protein synthesis.
