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A more recent version of this article appeared on October 29, 2004
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M407562200v1
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Papers In Press, published online ahead of print August 16, 2004
J. Biol. Chem, 10.1074/jbc.M407562200
Submitted on July 7, 2004
Revised on August 16, 2004
Accepted on August 16, 2004

Identification of a heme sensing domain in iron-regulatory protein 2

Jinsook Jeong, Tracey A. Rouault, and Rodney L. Levine

Laboratory of Biochemistry, NIH, Bethesda, MD 20892-0812

Corresponding Author: rlevine{at}nih.gov

Iron regulatory protein 2 coordinates cellular regulation of iron metabolism by binding to iron responsive elements in mRNA. The protein is synthesized constitutively but is rapidly degraded when iron stores are replete. The mechanisms which prevent degradation during iron deficiency or which promote degradation during iron sufficiency are not delineated. Iron regulatory protein 2 contains a domain not present in the closely related iron regulatory protein 1, and we found that this domain binds heme with high affinity. A cysteine within the domain is axially liganded to the heme, as occurs in cytochrome P450. The protein-bound heme reacts with molecular oxygen to mediate oxidation of cysteine, including beta-elimination of the sulfur to yield alanine. This covalent modification may thus mark the protein molecule for degradation by the proteasome system, providing another mechanism by which heme can regulate the level of iron regulatory protein 2.


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