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Vol. 12, No. 20, pp. 3236-3251, October 15, 1998
1 Department of Biochemistry, University of California,
Riverside, California 92521-0129 USA
The 5' leader (
) of tobacco mosaic viral RNA functions as a
translational enhancer. Sequence analysis of a 102-kD protein, identified previously as a specific RNA-binding protein, revealed homology to the HSP101/HSP104/ClpB family
of heat shock proteins and its expression in yeast complemented a
thermotolerance defect caused by a deletion of the HSP104 gene.
Up to a 50-fold increase in the translation of -luc, but not
luc mRNA was observed in yeast expressing the tobacco HSP101
whereas failed to enhance translation in the absence of HSP101.
Therefore, HSP101 and comprise a two-component translational
regulatory mechanism that can be recapitulated in yeast. Analysis of
HSP101 function in yeast translation mutants suggested that the
initiation factor (eIF) 3 and specifically one (TIF4632) of the two
eIF4G proteins were required for the HSP101-mediated enhancement. The
RNA-binding and translational regulatory activities of HSP101 were
inactive in respiring cells or in cells subject to nutrient limitation, but its thermotolerance function remained unaffected. This is the first
identification of a protein required for specific translational enhancement of capped mRNAs, the first report of a translational regulatory function for any heat-shock protein, and the first functional distinction between the two eIF4G proteins present in eukaryotes.
[Key Words: HSP101; translation initiation; protein synthesis; RNA-binding protein]
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