A regulated RNA binding protein also possesses aconitase activity

S. Kaptain, W. E. Downey, C. Tang, C. Philpott, D. Haile, D. G. Orloff, J. B. Harford, T. A. Rouault, R. D. Klausner

Research output: Contribution to journalArticle

155 Scopus citations

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 languageEnglish (US)
Pages (from-to)10109-10113
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number22
DOIs
StatePublished - Jan 1 1991
Externally publishedYes

Keywords

  • ferritin
  • iron
  • iron- responsive element binding protein
  • iron-responsive element
  • translational regulation

ASJC Scopus subject areas

  • General

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