A regulated RNA binding protein also possesses aconitase activity.

S Kaptain, William E. Downey, Catherine Tang, Carl Philpott, David J. Haile, David G. Orloff, Joe B. Harford, Tracey A. Rouault, Richard D. Klausner

Proceedings of the National Academy of Sciences · 1991 · 207 citations · 22 references

Concepts

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.

References

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