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Binding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA

Rouault, Tracey A., Hentze, Matthias W., Caughman, S. Wright, Harford, Joe B., Klausner, Richard D.·1988·Science

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Abstract

The human ferritin H chain messenger RNA contains a specific iron-responsive element (IRE) in its 5′ untranslated region, which mediates regulation by iron of ferritin translation. An RNA gel retardation assay was used to demonstrate the affinity of a specific cytosolic binding protein for the IRE. A single-base deletion in the IRE eliminated both the interaction of the cytoplasmic protein with the IRE and translational regulation. Thus, the regulatory potential of the IRE correlates with its capacity to specifically interact with proteins. Titration curves of binding activity after treatment of cells with an iron chelator suggest that the factor acts as a repressor of ferritin translation.

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Authors: Rouault, T. A., Hentze, M. W., Caughman, S. W., Harford, J. B., & Klausner, R. D.
Affiliations: National Institutes of Health (US)
ORCID: Rouault, Tracey A.
Hentze, Matthias W.
Harford, Joe B.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1988-09-02
Volume: 241
Issue: 4870
Pages: 1207-1210
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.3413484
OpenAlex: W2023361302
Cited by: 351
References: 16
Citations by year: 2026: 2 · 2025: 4 · 2024: 4 · 2023: 2 · 2022: 2 · 2021: 2 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 3 · 2014: 6 · 2013: 3 · 2012: 3
FWCI: 24.50
Type: journal article
Language: en
Open access: closed
Locations: Science (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: iron-responsive element, iron-responsive element-binding protein, translational regulation, 5' untranslated region, single-base deletion, iron chelators
MeSH terms: Base Composition, Binding, Competitive, Carrier Proteins, Cytosol, Deferoxamine, Ferritins, Globins, Humans, Iron, Liver, RNA, Messenger, Protein Biosynthesis, RNA-Binding Proteins, Nucleocytoplasmic Transport Proteins

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Binding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA

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