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. 1984 Oct 25;12(20):7889–7901. doi: 10.1093/nar/12.20.7889

tRNA binding modifies the properties of the small ribosomal subunit of rat liver.

A M Reboud, S Dubost, J P Reboud
PMCID: PMC320209  PMID: 6567844

Abstract

The binding of a specific tRNA (acylated or not) to the 40S subunits in the presence of the proper codon was shown to produce two striking effects on the subunits. First, the subunits were no longer able to dimerize at low ionic strength. Second, they became fully resistant to 1.25 M LiCl treatment: bound tRNA prevented subunit inactivation as measured by polyphenylalanine synthesis; it also prevented large sedimentation changes of subunits and ribosomal protein release induced by LiCl. The number of protected proteins far exceeded that of the proteins crosslinked with tRNA after irradiation at 254 nm (A.M. REBOUD, S. DUBOST and J.P. REBOUD (1983) FEBS Lett. 158, 285-288). These results strongly suggest that tRNA binding induces modifications of rRNA-protein interactions in large domains of the subunits. A weak interaction of tRNA with the 40S subunit was demonstrated in the absence of the codon.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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