Turning into a Frataxin-Independent Organism

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Frataxin was discovered because mutations in the corresponding gene cause the neurodegenerative disease Friedreich’s ataxia. The finding that frataxin protein physically associates with scaffold proteins Isu1/IscU places it squarely in the pathway of Fe-S cluster assembly. Fe-S clusters are essential cofactors for many proteins involved in cellular respiration, DNA repair, translation and other processes. Frataxin is conserved throughout evolution, being present in eukaryotes such as yeast and human and in some prokaryotes including E. coli. However, differences exist between the eukaryotic and prokaryotic forms of frataxin. The eukaryotic forms are critical for Fe-S cluster assembly whereas prokaryotic forms are more dispensable. We found that a key to this difference is a single amino acid in the scaffold protein Isu1 at position 141. Changes of the eukaryotic amino acid, Met, to prokaryotic amino acids, Ile, Leu, Cys, or Val, rendered mitochondria more frataxin-independent. No other changes were able to replicate this effect. Thus, Isu1 containing Met at position 141 may have coevolved with frataxin in eukaryotes, conferring frataxin-dependence. In contrast, the appearance of other amino acids at this position may have rendered prokaryotic cells less dependent on frataxin.

Vyšlo v časopise: Turning into a Frataxin-Independent Organism. PLoS Genet 11(5): e32767. doi:10.1371/journal.pgen.1005135
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005135

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