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.
MeSH Terms
Animals
Chromatography, DEAE-Cellulose
Chromatography, Gel
Ferritins/genetics
Mice
Molecular Weight
Protein Biosynthesis
RNA, Messenger/metabolism
Rabbits
Repressor Proteins/isolation & purification
Reticulocytes/analysis
Transcription Factors/isolation & purification
Ultracentrifugation
Chemicals
RNA, Messenger
Repressor Proteins
Transcription Factors
Ferritins
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Walden W E
Department of Microbiology and Immunology, College of Medicine, University of Illinois, Chicago 60612.
Daniels-McQueen S
Brown P H
Gaffield L
Russell D A
Bielser D
Bailey L C
Thach R E
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