Cited by 182Iron Metabolism and DisordersRNA and protein synthesis mechanismsRNA Research and Splicing

Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase

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Hentze, Matthias W., Argos, Patrick·1991·Nucleic Acids Research

Abstract

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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Crossref · 10.1093/nar/19.8.1739

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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
Venue
Nucleic Acids Research
Published
1991
Volume
19
Issue
8
Pages
1739-1740
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
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
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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