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. 1988 Dec;85(24):9503-7.
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, P H Brown, L Gaffield, D A Russell, D Bielser, L C Bailey, R E Thach
Affiliations

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

W E Walden et al. Proc Natl Acad Sci U S A. 1988 Dec.

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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