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Nucleic Acids Research, 1988, Vol. 16, No. 17 8675-8694
© 1988

Articles

The ribosomal fraction mediates the translational enhancement associated with the 5'-leader of tobacco mosaic virus

Daniel R. Gallic*, Virginia Walbot and John W.B. Hershey1

Department of Biological Sciences, Stanford University Stanford, CA 94305, USA 1Department of Biological Chemistry, University of California Davis, CA 95616, USA

*To whom correspondence should be addressed

Received April 11, 1988. Revised July 26, 1988. Accepted July 26, 1988.

The ohm sequence at the 5'-terminus of tobacco mosaic virus (TMV) RNA acts as a translational enhancer. The differential in ohm-associated translational enhancement between the in vitro translation system derived from wheat germ (WG) and that from rabbit reticulocytes (MDL) was exploited to identify that lysate component which was responsible for a lysate's characteristic reponse to ohm. Using fractionated MDL and WG lysates, which were reconstituted in various combinations, the high salt-washed ribosomal fraction was determined to be the responsive element in a lysate. Analysis of ohm's ability to enhance translation was greatest at low mRNA and high ribosomal concentrations and to occur in the early phase of an in vitro translation assay. Translation of ohm-containing CAT mRNA was more sensitive to the presence of micrococcal nuclease than CAT mRNA without an ohm. In substitution experiments, WG ribosomes functioned at much reduced efficiency in MDL as did MDL ribosomes in WG lysate. The initiation factor-containing fraction of one system could not, as a whole, functionally replace that of the other and actually acted to inhibit translation in the heterologous system.


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