Abstract
A clone for the iron-responsive element (IRE)-binding protein (IRE-BP) has been transfected and expressed in mouse fibroblasts. The IRE-BP gene product binds IREs with high affinity and specificity. Amino acid alignments reveal that the IRE-BP is 30% identical to mitochondrial aconitase. The 18 active site residues of mitochondrial aconitase are identical to those in the IRE- BP, suggesting that the IRE-BP may possess aconitase activity. After purification of native IRE-BP and immunoaffinity purification of transfected and expressed IRE-BP, we demonstrate that the purified IRE-BP has aconitase activity.
Original language | English (US) |
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Pages (from-to) | 10109-10113 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 88 |
Issue number | 22 |
DOIs | |
State | Published - 1991 |
Externally published | Yes |
Keywords
- ferritin
- iron
- iron- responsive element binding protein
- iron-responsive element
- translational regulation
ASJC Scopus subject areas
- General