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FEBS J. 2009 Nov;276(22):6669-76. doi: 10.1111/j.1742-4658.2009.07381.x. Epub 2009 Oct 16.

The N-terminus of mature human frataxin is intrinsically unfolded.

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  • 1Dipartimento di Biologia Molecolare, University of Siena, Siena, Italy.


Frataxin is a highly conserved nuclear-encoded mitochondrial protein whose deficiency is the primary cause of Friedreich's ataxia, an autosomal recessive neurodegenerative disease. The frataxin structure comprises a well-characterized globular domain that is present in all species and is preceded in eukaryotes by a non-conserved N-terminal tail that contains the mitochondrial import signal. Little is known about the structure and dynamic properties of the N-terminal tail. Here, we show that this region is flexible and intrinsically unfolded in human frataxin. It does not alter the iron-binding or self-aggregation properties of the globular domain. It is therefore very unlikely that this region could be important for the conserved functions of the protein.

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