Key result
The RPS18C leader sequence mediated cap-independent translation in an in vitro wheat germ extract system, which was inhibited by an oligonucleotide competing for the 18S rRNA site.
The RPS18C leader sequence mediates cap-independent translation in vitro, which is dependent on complementarity to the 18S rRNA.
No immediate clinical implications; leaves open conservation of rRNA-mediated translation in mammalian systems.
Cap-independent translation (CIT) occurs at the leader sequences of uncapped plant viral RNAs, but also at a number of normally capped cellular mRNAs and has been correlated with sequence complementarity to 18S rRNA. The ribosomal protein S18 (RPS18) is a component of the small ribosomal subunit and is encoded by three gene copies (A, B, and C) in the Arabidopsis thaliana genome. The RPS18C mRNA was most abundant and contained a short 5' untranslated region of 84 bp that is complementary to a novel putative interaction site at the 3' end of the 18S rRNA. The RPS18C leader mediated CIT as demonstrated by dicistronic constructs consisting of luciferase and chloramphenicol acetyl transferase reporter genes in an in vitro wheat germ extract system. CIT was rapidly inhibited upon addition of an oligonucleotide that competed for the 18S rRNA site complementary to the RPS18C leader and interfered with polysome assembly at the transcript.
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Vanderhaeghen et al. (2006) studied this question. RPS18C leader sequence was evaluated on Cap-independent translation (CIT). The RPS18C leader sequence mediated cap-independent translation in an in vitro wheat germ extract system, which was inhibited by an oligonucleotide competing for the 18S rRNA site.
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