RGD Reference Report - Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. - Rat Genome Database

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Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity.

Authors: Bulteau, AL  O'Neill, HA  Kennedy, MC  Ikeda-Saito, M  Isaya, G  Szweda, LI 
Citation: Bulteau AL, etal., Science 2004 Jul 9;305(5681):242-5.
RGD ID: 1304347
Pubmed: (View Article at PubMed) PMID:15247478
DOI: Full-text: DOI:10.1126/science.1098991

Numerous degenerative disorders are associated with elevated levels of prooxidants and declines in mitochondrial aconitase activity. Deficiency in the mitochondrial iron-binding protein frataxin results in diminished activity of various mitochondrial iron-sulfur proteins including aconitase. We found that aconitase can undergo reversible citrate-dependent modulation in activity in response to pro-oxidants. Frataxin interacted with aconitase in a citrate-dependent fashion, reduced the level of oxidant-induced inactivation, and converted inactive [3Fe-4S]1+ enzyme to the active [4Fe-4S]2+ form of the protein. Thus, frataxin is an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Fxn  (frataxin)

Objects referenced in this article
0 Aco2 aconitase 2 All species

Additional Information