Open AccessA regulated RNA binding protein also possesses aconitase activity.
Author(s) -
Stamatina Kaptain,
William Downey,
Catherine Tang,
Caroline C. Philpott,
David J. Haile,
David G. Orloff,
Joe B. Harford,
Tracey A. Rouault,
Richard D. Klausner
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.22.10109
Subject(s) - aconitase , internal ribosome entry site , transfection , clone (java method) , mitochondrion , chemistry , biology , biochemistry , rna , microbiology and biotechnology , gene , ribosome
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.