Abstract
Abstract The effect of subunit I, an acidic protein isolated from the 1.0 m NH4Cl wash of Escherichia coli MRE 600, on the translation of synthetic and natural mRNA was investigated. In addition to R17 RNA and poly(U) translation, subunit I strongly inhibited amino acid incorporation directed by synthetic polynucleotides containing a high proportion of pyrimidines. Inhibition of translation was independent of the time of addition of this factor to the reaction. The amount of inhibition by subunit I of either poly(U) or R17 RNA translation was a sensitive function of the messenger concentration in the assay. A stable complex of subunit I and ribosomes was isolated and was found to have reduced activity in messenger translation. No interaction of subunit I with IF-3 could be demonstrated either in messenger translation or in dissociation of single ribosomes. Endogenous E. coli mRNA translation and ApUpG-dependent binding of f[14C]Met-tRNA to ribosomes were unaffected by this protein.
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