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

doi:10.1073/pnas.88.22.10109

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 journal › Article › peer-review

156 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 language	English (US)
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	https://doi.org/10.1073/pnas.88.22.10109
State	Published - 1991
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

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10.1073/pnas.88.22.10109

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A regulated RNA binding protein also possesses aconitase activity. / Kaptain, S.; Downey, W. E.; Tang, C.; Philpott, C.; Haile, D.; Orloff, D. G.; Harford, J. B.; Rouault, T. A.; Klausner, R. D.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 22, 1991, p. 10109-10113.

Research output: Contribution to journal › Article › peer-review

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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.",

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AU - Kaptain, S.

AU - Downey, W. E.

AU - Tang, C.

AU - Philpott, C.

AU - Haile, D.

AU - Orloff, D. G.

AU - Harford, J. B.

AU - Rouault, T. A.

AU - Klausner, R. D.

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AB - 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.

KW - ferritin

KW - iron

KW - iron- responsive element binding protein

KW - iron-responsive element

KW - translational regulation

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A regulated RNA binding protein also possesses aconitase activity

Abstract

Keywords

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