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. 1988 Dec;85(24):9503–9507. doi: 10.1073/pnas.85.24.9503

Translational repression in eukaryotes: partial purification and characterization of a repressor of ferritin mRNA translation.

W E Walden 1, S Daniels-McQueen 1, P H Brown 1, L Gaffield 1, D A Russell 1, D Bielser 1, L C Bailey 1, R E Thach 1
PMCID: PMC282781  PMID: 3200835

Abstract

Mouse and rabbit ferritin mRNAs translate very poorly in rabbit reticulocyte lysates relative to most other mRNAs. This translational deficiency is not seen in wheat germ lysates, suggesting the presence of an inhibitor in reticulocyte lysate that is specific for ferritin mRNA. A specific repressor of ferritin mRNA translation has been partially purified from rabbit reticulocytes by differential ultracentrifugation, ammonium sulfate fractionation, and chromatography on phosphocellulose, DEAE-cellulose, and Sephacryl S-300. The elution profile from the latter suggests an aggregate molecular mass of approximately 180 kDa for the repressor. The inhibitory activity of this repressor against native ferritin mRNA can be relieved by adding in vitro transcripts of ferritin light-chain RNAs that contain the first 92 nucleotides of the 5' untranslated region. No other sequences appear to be necessary for this effect.

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