Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase
Open accessAbstract
Iron-responsive elements (IREs) are regulatory RNA elements which serve as specific binding sites for the IRE-binding protein (IRE-BP). Interaction between IREs and IRE-BP induces repression of ferritin mRNA translation and transferrin receptor mRNA stabilization. We describe the identification of extensive amino acid sequence homology between IRE-BP and two known isomerases, aconitase and isopropylmalate (IPM) isomerase. We discuss the implications of this observation with regard to structure/function relationships of IRE-BP. The structural conservation between a regulatory RNA-binding protein and two enzymes involved in intermediary metabolism provides a surprising example of the functional flexibility in biological structures.
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- Authors
- Hentze, M. W., & Argos, P.
- Affiliations
- European Molecular Biology Laboratory (DE)
- European Molecular Biology Laboratory (ES)
- Corresponding author
- Argos, Patrick
- ORCID
- Hentze, Matthias W.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1991
- Volume
- 19
- Issue
- 8
- Pages
- 1739-1740
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC328097
- OpenAlex
- W1971099877
- Cited by
- 182
- References
- 22
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 8 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 1 · 2018: 4 · 2017: 3 · 2016: 4 · 2015: 2 · 2014: 9 · 2013: 5 · 2012: 3
- FWCI
- 13.22
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Nucleic Acids Research (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
- iron-responsive element, aconitase, sequence homology, RNA-binding proteins, structure-function relationship, iron metabolism regulation
- MeSH terms
- Aconitate Hydratase, Amino Acid Sequence, Animals, Carrier Proteins, Humans, Isomerases, Molecular Sequence Data, RNA, Messenger, Sequence Homology, Nucleic Acid, Sequence Alignment, RNA-Binding Proteins, Iron-Regulatory Proteins
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