Journal
EMBO REPORTS
Volume 5, Issue 11, Pages 1096-1101Publisher
WILEY
DOI: 10.1038/sj.embor.7400272
Keywords
frataxin; Yfh1; mitochondria; iron; oligomerization
Categories
Funding
- NIGMS NIH HHS [R01 GM027870, GM27870] Funding Source: Medline
- PHS HHS [5T326M08349] Funding Source: Medline
Ask authors/readers for more resources
The neurodegenerative disease Friedreich's ataxia is caused by reduced levels of frataxin, a mitochondrial matrix protein. The in vivo role of frataxin is under debate. Frataxin, as well as its yeast homologue Yfh1, binds multiple iron atoms as an oligomer and has been proposed to function as a crucial iron-storage protein. We identified a mutant Yfh1 defective in iron-induced oligomerization. This mutant protein was able to replace functionally wild-type Yfh1, even when expressed at low levels, when mitochondrial iron levels were high and in mutant strains having deletions of genes that had synthetic growth defects with a YFH1 deletion. The ability of an oligomerization-deficient Yfh1 to function in vivo suggests that oligomerization, and thus oligomerization-induced iron storage, is not a critical function of Yfh1. Rather, the capacity of this oligomerization-deficient mutant to interact with the Isu protein suggests a more direct role of Yfh1 in iron-sulphur cluster biogenesis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available