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Title:
Coordinating responses to iron and oxygen stress with DNA and mRNA promoters: The ferritin story | BioMetals
Description:
Combinations of DNA antioxidant response element and mRNA iron responsive element regulate ferritin expression in animals in response to oxidant and iron stress, or normal developmental signals. Ferritins are protein nanocages, found in animals, plants, bacteria, and archaea, that convert iron and oxygen to ferric oxy biominerals in the protein central cavity; the mineral traps potentially toxic reactants and concentrates iron for the future synthesis of other iron/heme proteins. Regulatory signals and the nanocage gene products are the same throughout biology, but the genetic mechanisms, DNA versus DNA + mRNA, vary. The number of genes, temporal regulation, tissue distribution in multi-cellular organisms, and gene product size (maxi-ferritins have 24 subunits and mini-ferritins, or Dps proteins, have 12 subunits and are restricted to bacteria and archaea) suggest an overwhelming diversity and variability. However, common themes of regulation and function are described which indicate not only that the three-dimensional protein structure and the functions of the ferritins are conserved, but also that broad features of genetic regulation are conserved relative to organismal and/or community needs. The analysis illustrates the centrality of the ferritins to life with iron and oxygen and models how Nature harnesses potentially dangerous chemistry for biology.
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Keywords {š}
article, google, scholar, cas, pubmed, iron, ferritin, theil, biol, protein, regulatory, regulation, chem, mrna, gene, usa, sci, element, structure, plant, acad, dna, expression, proteins, binding, proc, natl, oxygen, ferritins, genes, rna, mol, cells, content, stress, privacy, cookies, research, biometals, responses, antioxidant, response, bacteria, dps, soybean, cell, function, analysis, publish, search,
Topics {āļø}
starvation-induced dps/pexb-homologous gene month download article/chapter iso-iron responsive elements conserved iron-responsive elements nf-e2-related factors base-paired flanking regions protein-coated iron minerals metal-catalysed histidine oxidation cap-binding complex eif4f iron-sulphur cluster biogenesis nuclear receptor-coactivator interactions ferritin gene transcription long-term iron overload iron-responsive degradation ire/irp regulatory system nanocage gene products iron regulatory proteins full article pdf iron-dependent regulation iron regulatory element internal loop/bulge structure dna-binding protein antioxidant response element article biometals aims iron-regulatory protein 1 iron-regulatory protein 2 anthracis dps proteins gene product size privacy choices/manage cookies iron/heme proteins heme oxygenase-1 gene siderophore-mediated upregulation iron-controlling genes rna binding sites rna binding form cytoprotective antioxidant strategem protein central cavity opening protein pores related subjects coordinating responses mrna loop/bulge arabidopsis ferritin expression metal ion stress mrna elements cellular iron homeostasis mitochondrial iron homeostasis european economic area ferric oxy biominerals erwinia chrysanthemi infection hypoxia-inducible repressor
Questions {ā}
- Grotz N, Guerinot ML (2002) Limiting nutrients: an old problem with new solutions?
- Ke Y, Wu J, Leibold EA, Walden WE, Theil EC (1998) Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding: fine-tuning of mRNA regulation?
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headline:Coordinating responses to iron and oxygen stress with DNA and mRNA promoters: The ferritin story
description:Combinations of DNA antioxidant response element and mRNA iron responsive element regulate ferritin expression in animals in response to oxidant and iron stress, or normal developmental signals. Ferritins are protein nanocages, found in animals, plants, bacteria, and archaea, that convert iron and oxygen to ferric oxy biominerals in the protein central cavity; the mineral traps potentially toxic reactants and concentrates iron for the future synthesis of other iron/heme proteins. Regulatory signals and the nanocage gene products are the same throughout biology, but the genetic mechanisms, DNA versus DNA + mRNA, vary. The number of genes, temporal regulation, tissue distribution in multi-cellular organisms, and gene product size (maxi-ferritins have 24 subunits and mini-ferritins, or Dps proteins, have 12 subunits and are restricted to bacteria and archaea) suggest an overwhelming diversity and variability. However, common themes of regulation and function are described which indicate not only that the three-dimensional protein structure and the functions of the ferritins are conserved, but also that broad features of genetic regulation are conserved relative to organismal and/or community needs. The analysis illustrates the centrality of the ferritins to life with iron and oxygen and models how Nature harnesses potentially dangerous chemistry for biology.
datePublished:2007-01-09T00:00:00Z
dateModified:2007-01-09T00:00:00Z
pageStart:513
pageEnd:521
sameAs:https://doi.org/10.1007/s10534-006-9063-6
keywords:
Oxygen
Ferritin
Dps protein
Antioxidant response (ARE) genes
mRNA (IRE) regulation
Biochemistry
general
Pharmacology/Toxicology
Microbiology
Cell Biology
Plant Physiology
Medicine/Public Health
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headline:Coordinating responses to iron and oxygen stress with DNA and mRNA promoters: The ferritin story
description:Combinations of DNA antioxidant response element and mRNA iron responsive element regulate ferritin expression in animals in response to oxidant and iron stress, or normal developmental signals. Ferritins are protein nanocages, found in animals, plants, bacteria, and archaea, that convert iron and oxygen to ferric oxy biominerals in the protein central cavity; the mineral traps potentially toxic reactants and concentrates iron for the future synthesis of other iron/heme proteins. Regulatory signals and the nanocage gene products are the same throughout biology, but the genetic mechanisms, DNA versus DNA + mRNA, vary. The number of genes, temporal regulation, tissue distribution in multi-cellular organisms, and gene product size (maxi-ferritins have 24 subunits and mini-ferritins, or Dps proteins, have 12 subunits and are restricted to bacteria and archaea) suggest an overwhelming diversity and variability. However, common themes of regulation and function are described which indicate not only that the three-dimensional protein structure and the functions of the ferritins are conserved, but also that broad features of genetic regulation are conserved relative to organismal and/or community needs. The analysis illustrates the centrality of the ferritins to life with iron and oxygen and models how Nature harnesses potentially dangerous chemistry for biology.
datePublished:2007-01-09T00:00:00Z
dateModified:2007-01-09T00:00:00Z
pageStart:513
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sameAs:https://doi.org/10.1007/s10534-006-9063-6
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Oxygen
Ferritin
Dps protein
Antioxidant response (ARE) genes
mRNA (IRE) regulation
Biochemistry
general
Pharmacology/Toxicology
Microbiology
Cell Biology
Plant Physiology
Medicine/Public Health
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