Cytoplasmic Protein Binds in vitro to a Highly Conserved Sequence in the 5′ Untranslated Region of Ferritin Heavy- and Light-Subunit mRNAs

The mRNAs for the heavy and light subunits of the iron-storage protein ferritin occur in cells largely as inactive ribonucleoprotein particles, which are recruited for translation when iron enters the cell. Cytoplasmic extracts from rat tissues and hepatoma cells were shown by an electrophoretic sep...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-04, Vol.85 (7), p.2171-2175
Main Authors: Leibold, Elizabeth A., Munro, Hamish N.
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Carrier Proteins - metabolism
Chemical bases
Conserved sequences
Ferritins
Ferritins - biosynthesis
Ferritins - genetics
Fundamental and applied biological sciences. Psychology
Gels
Gene expression
Gene Expression Regulation
Heparin
Hepatocellular carcinoma
Introns
Iron - pharmacology
Liver
Liver - analysis
Liver Neoplasms, Experimental
Male
Messenger RNA
Molecular and cellular biology
Molecular genetics
Myocardium - analysis
Rats
Rats, Inbred Strains
RNA
RNA Processing, Post-Transcriptional
RNA, Messenger - metabolism
RNA-Binding Proteins
Tumor Cells, Cultured - analysis
Untranslated regions
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The mRNAs for the heavy and light subunits of the iron-storage protein ferritin occur in cells largely as inactive ribonucleoprotein particles, which are recruited for translation when iron enters the cell. Cytoplasmic extracts from rat tissues and hepatoma cells were shown by an electrophoretic separation procedure to form RNA-protein complexes involving a highly conserved sequence in the 5′ untranslated region of both ferritin heavy- and light-subunit mRNAs. The pattern of complex formation was affected by pretreatment of rats or cells with iron. Crosslinking by UV irradiation showed that the complexes contained an 87-kDa protein interacting with the conserved sequence of the ferritin mRNA. We propose that intracellular iron levels regulate ferritin synthesis by causing changes in specific protein binding to the conserved sequence in the ferritin heavy- and light-subunit mRNAs.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.7.2171