ArticleNucleic acids research1995
Role of RNA secondary structure of the iron-responsive element in translational regulation of ferritin synthesis.
Article in Nucleic acids research, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 45 citations in OpenAlex.
- Sequence alignment of the primate lineage reveals evolutionary divergence and conserved secondary structural motifs in noncoding RNAs.bioRxiv : the preprint server for biology · 2026Article
- Identification of RNA structures and their roles in RNA functions.Nature reviews. Molecular cell biology · 2024Review
- Review
- Sensitive measurement of single-nucleotide polymorphism-induced changes of RNA conformation: application to disease studies.Nucleic acids research · 2013Article
- Iron responsive mRNAs: a family of Fe2+ sensitive riboregulators.Accounts of chemical research · 2011Article
- Multiple determinants within iron-responsive elements dictate iron regulatory protein binding and regulatory hierarchy.RNA (New York, N.Y.) · 2010Article
- Targeting the progression of Parkinson's disease.Current neuropharmacology · 2009Article
- The functional duality of iron regulatory protein 1.Current opinion in structural biology · 2008Review
- Iron responsive element RNA flexibility described by NMR and isotropic reorientational eigenmode dynamics.Journal of biomolecular NMR · 2005Article
- Dynamics of the IRE RNA hairpin loop probed by 2-aminopurine fluorescence and stochastic dynamics simulations.RNA (New York, N.Y.) · 2004Article
- In vitro selection of an RNA sequence that interacts with high affinity with thymidylate synthase.Nucleic acids research · 2000Article
- A macrocyclic bis-acridine shifts the equilibrium from duplexes towards DNA hairpins.Nucleic acids research · 1997Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Iron regulates synthesis of the iron storage protein ferritin at the translational level through interaction between a stem-loop structure, the iron-responsive element (IRE), located in the 5'-untranslated region (5'-UTR) of ferritin mRNAs, and a protein, the iron regulatory protein (IRP). The role of IRE secondary structure in translational regulation of ferritin synthesis was explored by introducing ferritin constructs containing mutations in the IRE into Rat-2 fibroblasts. Our in vivo studies demonstrate that size and sequence of the loop within the IRE and the distance and/or spatial relationship of this loop to the bulged nucleotide region closest to the loop must be preserved in order to observe iron-dependent translation of ferritin mRNA. In contrast, changes in nucleotide sequence of the upper stem can be introduced without affecting translational regulation in vivo, as long as a stem can be formed. Our in vivo results suggest that only a very small variation in the affinity of interaction of IRP with IRE can be tolerated in order to maintain iron-dependent regulation of translation.
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