The N-terminus of mature human frataxin is intrinsically unfolded
Authors: Prischi, Filippo1; Giannini, Clelia2; Adinolfi, Salvatore3; Pastore, Annalisa3
Source: FEBS Journal, Volume 276, Number 22, November 2009 , pp. 6669-6676(8)
Publisher: Blackwell Publishing
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Abstract:
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.Keywords: dynamics; Friedreich's ataxia; IUPs; NMR; structure
Document Type: Research article
DOI: 10.1111/j.1742-4658.2009.07381.x
Affiliations: 1: Dipartimento di Biologia Molecolare, University of Siena, Siena, Italy 2: Dipartimento di Chimica Organica ed Industriale, University of Milano, Italy 3: National Institute for Medical Research, MRC, The Ridgeway, London, UK
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