The N-terminus of mature human frataxin is intrinsically unfolded.
- Resource Type
- Article
- Authors
- Prischi, Filippo; Giannini, Clelia; Adinolfi, Salvatore; Pastore, Annalisa
- Source
- FEBS Journal. Nov2009, Vol. 276 Issue 22, p6669-6676. 8p. 5 Graphs.
- Subject
- *PROTEINS
*FRIEDREICH'S ataxia
*NEURODEGENERATION
*PATHOLOGY
*MOVEMENT disorders
- Language
- ISSN
- 1742-464X
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. [ABSTRACT FROM AUTHOR]