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  • 1
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    Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rouault, T A -- Hentze, M W -- Caughman, S W -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1207-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413484" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Binding, Competitive ; Carrier Proteins/*metabolism ; Cytosol/analysis ; Deferoxamine/pharmacology ; Ferritins/*genetics ; Globins/genetics ; Humans ; Iron/*pharmacology ; Liver/analysis ; *Nucleocytoplasmic Transport Proteins ; Protein Biosynthesis/drug effects ; RNA, Messenger/*metabolism ; *RNA-Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-21
    Description: Iron-responsive elements (IREs) are RNA motifs that have been identified within the 5' untranslated region of ferritin messenger RNA and the 3' untranslated region of transferrin receptor mRNA. A single IRE mediates iron-dependent control of ferritin translation, whereas multiple IREs are found in the region of the transferrin receptor mRNA responsible for iron-dependent control of mRNA stability. A cytosolic protein binds in vitro to the IREs of both mRNAs. The IRE-binding protein (IRE-BP) is shown to require free sulfhydryl groups for its specific interaction with the IRE. Treatment of lysates with reducing agents increases the binding activity, whereas agents that block sulfhydryls inhibit binding. Iron starvation, leading to decreased ferritin translation, results in increased binding activity, which is explained by an increase in the fraction of the IRE-BP that is in a fully reduced state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- Rouault, T A -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1989 Apr 21;244(4902):357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2711187" target="_blank"〉PubMed〈/a〉
    Keywords: Cytosol/metabolism ; DNA-Binding Proteins/*metabolism ; Disulfides/metabolism ; Dithiothreitol/pharmacology ; Ethylmaleimide/pharmacology ; Ferritins/*genetics ; Humans ; Iron/*pharmacology ; Leukemia, Erythroblastic, Acute ; Mercaptoethanol/pharmacology ; Oxidation-Reduction ; Protein Biosynthesis/drug effects ; RNA, Messenger/genetics/*metabolism ; Receptors, Transferrin/*genetics ; Regulatory Sequences, Nucleic Acid ; Sulfhydryl Compounds/metabolism ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Cell biology. An ancient gauge for iron (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-11
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2932448/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2932448/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rouault, Tracey A -- ZIA HD001602-25/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2009 Oct 30;326(5953):676-7. doi: 10.1126/science.1181938.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Medicine Program, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA. trou@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19900922" target="_blank"〉PubMed〈/a〉
    Keywords: Cytosol/metabolism ; F-Box Proteins/chemistry/*metabolism ; Hemerythrin/metabolism ; Homeostasis ; Humans ; Iron/*metabolism ; Iron Regulatory Protein 1/metabolism ; Iron Regulatory Protein 2/metabolism ; RNA, Messenger/metabolism ; Ubiquitin-Protein Ligases/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Microbiology. Pathogenic bacteria prefer heme (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rouault, Tracey A -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1577-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Human Iron Metabolism, Cell Biology and Metabolism Branch, the National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. trou@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15361615" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antimicrobial Cationic Peptides/metabolism ; Bloodletting ; Caenorhabditis elegans/microbiology ; Heme/*metabolism ; Hemoglobins/metabolism ; Hepcidins ; Humans ; Iron/blood/*metabolism ; Iron Isotopes ; Membrane Transport Proteins/genetics/metabolism ; Mice ; Staphylococcal Infections/microbiology ; Staphylococcus aureus/genetics/growth & development/*metabolism/*pathogenicity ; Transferrin/metabolism ; Virulence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: The iron-regulatory proteins (IRPs) posttranscriptionally regulate expression of transferrin receptor, ferritin, and other iron metabolism proteins. Although both IRPs can regulate expression of the same target genes, IRP2-/- mice significantly misregulate iron metabolism and develop neurodegeneration, whereas IRP1-/- mice are spared. We found that IRP2-/- cells misregulated iron metabolism when cultured in 3 to 6% oxygen, which is comparable to physiological tissue concentrations, but not in 21% oxygen, a concentration that activated IRP1 and allowed it to substitute for IRP2. Thus, IRP2 dominates regulation of mammalian iron homeostasis because it alone registers iron concentrations and modulates its RNA-binding activity at physiological oxygen tensions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyron-Holtz, Esther G -- Ghosh, Manik C -- Rouault, Tracey A -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2087-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604406" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Ferritins/biosynthesis/metabolism ; Gene Expression Regulation ; Homeostasis ; Iron/*metabolism ; Iron Regulatory Protein 1/genetics/*metabolism ; Iron Regulatory Protein 2/genetics/*metabolism ; Lymphocytes/*metabolism ; Macrophages/*metabolism ; Mice ; Oxidants/metabolism ; Oxygen/*physiology ; RNA/metabolism ; Receptors, Transferrin/biosynthesis/metabolism ; Response Elements ; Spleen/cytology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Biochemistry. If the RNA fits, use it (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rouault, Tracey A -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1886-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA. trou@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185590" target="_blank"〉PubMed〈/a〉
    Keywords: Apoferritins/*genetics ; Apoproteins/chemistry/metabolism ; Crystallography, X-Ray ; Evolution, Molecular ; Iron/metabolism ; Iron Regulatory Protein 1/*chemistry/*metabolism ; Ligands ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/metabolism ; *Regulatory Sequences, Ribonucleic Acid ; *Response Elements ; Sulfur/metabolism ; Untranslated Regions/*chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Identification of the iron-responsive element for the translational regulation of human ferritin mRNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-11
    Description: Regulated translation of messenger RNA offers an important mechanism for the control of gene expression. The biosynthesis of the intracellular iron storage protein ferritin is translationally regulated by iron. A cis-acting element that is both necessary and sufficient for this translational regulation is present within the 5' nontranslated leader region of the human ferritin H-chain messenger RNA. In this report the iron-responsive element (IRE) was identified by deletional analysis. Moreover, a synthetic oligodeoxynucleotide was shown to be able to transfer iron regulation to a construct that would otherwise not be able to respond to iron. The IRE has been highly conserved and predates the evolutionary segregation between amphibians, birds, and man. The IRE may prove to be useful for the design of translationally regulated expression systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- Caughman, S W -- Rouault, T A -- Barriocanal, J G -- Dancis, A -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1570-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685996" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; Ferritins/*genetics ; *Gene Expression Regulation ; Genes ; Humans ; Iron/*pharmacology ; Molecular Sequence Data ; Plasmids ; Promoter Regions, Genetic/*drug effects ; *Protein Biosynthesis ; RNA, Messenger/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-13
    Description: The biosynthetic rates for both the transferrin receptor (TfR) and ferritin are regulated by iron. An iron-responsive element (IRE) in the 5' untranslated portion of the ferritin messenger RNA (mRNA) mediates iron-dependent control of its translation. In this report the 3' untranslated region of the mRNA for the human TfR was shown to be necessary and sufficient for iron-dependent control of mRNA levels. Deletion studies identified a 678-nucleotide fragment of the TfR complementary DNA that is critical for this iron regulation. Five potential stem-loops that resemble the ferritin IRE are contained within the region critical for TfR regulation. Each of two of the five TfR elements was independently inserted into the 5' untranslated region of an indicator gene transcript. In this location they conferred iron regulation of translation. Thus, an mRNA element has been implicated in the mediation of distinct regulatory phenomena dependent on the context of the element within the transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casey, J L -- Hentze, M W -- Koeller, D M -- Caughman, S W -- Rouault, T A -- Klausner, R D -- Harford, J B -- New York, N.Y. -- Science. 1988 May 13;240(4854):924-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2452485" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics ; DNA, Recombinant ; Ferritins/biosynthesis/*genetics ; Growth Hormone/genetics ; Humans ; Iron/*pharmacology ; Mice ; Plasmids ; Protein Biosynthesis/*drug effects ; RNA/*genetics ; RNA, Messenger/*genetics ; Receptors, Transferrin/biosynthesis/*genetics ; *Regulatory Sequences, Nucleic Acid ; Transcription, Genetic ; Transfection ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
    Electronic Resource
    Electronic Resource
    Post-transcriptional regulation of genes of iron metabolism in mammalian cells (1996)
    Springer
    JBIC 1 (1996), S. 494-499 
    Details
    ISSN: 1432-1327
    Keywords: Key words Iron ; Iron-sulfur proteins ; Aconitase ; IRE ; IRP1 and IRP2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  Iron metabolism is tightly regulated in mammalian cells. Here we describe several types of post-transcriptional mechanisms that have been identified in regulation of genes of iron metabolism. Iron-dependent regulation of stability of the transcript is the key to regulation of the expression of the transferrin receptor. Selective repression of translation in iron-depleted cells is the key to regulation of the expression of ferritin and several other genes that require iron for function. Specific regulatory proteins that directly sense iron levels in cells are needed to coordinate iron metabolism. These proteins, known as iron regulatory proteins (IRPs), bind to specific RNA stem-loops in transcripts with high affinity when cells are depleted of iron. The two IRPS, IRP1 and IRP2, are post-translationally modified by iron, but the nature of the post-translational regulatory process differs. IRP1 assembles an iron-sulfur cluster which determines its function, whereas IRP2 is rapidly degraded in the presence of iron. Direct binding of iron is likely to be involved in sensing of iron levels by IRP1 and IRP2. Although each IRP binds to the RNA stem-loop motifs known as iron-responsive elements (IREs) with high affinity, it is possible that each protein binds an additional, unique set of target-binding motifs. The list of potential genes that are regulated by IRPs continues to grow, and much remains to be learned about the regulation of mammalian iron metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050083
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  • 10
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    Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster (2003)
    National Academy of Sciences
    Details
    Publication Date: 2003-07-28
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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