Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs.

Leibold, E A; Munro, H N

doi:10.1073/pnas.85.7.2171

Cited by 671Iron Metabolism and DisordersRNA and protein synthesis mechanismsRNA Research and Splicing

Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs.

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Leibold, E A, Munro, H N·1988·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.85.7.2171PMC PMC279951

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Abstract

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.

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Cytoplasmic proteins now known as iron regulatory proteins (IRPs) recognize and bind to the IREs.
“Soon afterward it was shown that cytoplasmic proteins, now known as iron regulatory proteins (IRPs, formerly IREBPs), recognize and bind to the IREs.”
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Jong, J. G. T.-D., Brouwer, J., Rietveld, K., et al. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb02058.x · Cited by 18 · see citing works

Authors: Leibold, E. A., & Munro, H. N.
Affiliations: Massachusetts Institute of Technology (US)
ORCID: Leibold, E A
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1988-04
Volume: 85
Issue: 7
Pages: 2171-2175
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.85.7.2171
PMC: PMC279951
OpenAlex: W2085866164
Cited by: 671
References: 29
Citations by year: 2026: 3 · 2025: 6 · 2024: 2 · 2023: 5 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 3 · 2018: 5 · 2017: 8 · 2016: 4 · 2015: 4 · 2014: 9 · 2013: 3 · 2012: 6
FWCI: 31.36
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Keywords: ferritin, 5' untranslated region, conserved sequences, protein-RNA complex, cytosolic proteins, iron regulation, iron storage, translational regulation, ribonucleoprotein particles, UV crosslinking, hepatoma cells
MeSH terms: Animals, Carrier Proteins, Ferritins, Gene Expression Regulation, Introns, Iron, Liver, Liver Neoplasms, Experimental, Male, Myocardium, Rats, Inbred Strains, RNA Processing, Post-Transcriptional, RNA, Messenger, Tumor Cells, Cultured, RNA-Binding Proteins, Rats

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Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs.

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