Frataxin, a nuclear encoded protein targeted to the mitochondrial matrix, has recently been implicated as an iron chaperone that delivers ferrous iron to the iron-sulfur assembly enzyme IscU. During transport across the mitochondrial membrane, the N-terminal mitochondrial targeting sequence of frataxin is cleaved in a two-step process to produce the mature protein found in the matrix, however N-terminal extended forms of the protein have also been observed in vivo. The recent structural characterization studies of the human frataxin ortholog were performed on a truncated variant of the protein. Here we report the NMR spectral assignment of an extended form of the mature human frataxin ortholog as the basis for understanding the role of the N-terminal domain in protein function.
Biochemistry | Molecular Biology
Kondapalli KC, Bencze KZ et al (2010) NMR assignments of a stable processing intermediate of human frataxin. Biomol NMR Assign 4(1): 61-64 doi:10.1007/s12104-010-9209-x