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Mitochondrial functional interactions between frataxin and Isu1p, the iron–sulfur cluster scaffold protein, in Saccharomyces cerevisiae
Author(s) -
Ramazzotti Anna,
Vanmansart Vincent,
Foury Françoise
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01498-4
Subject(s) - frataxin , saccharomyces cerevisiae , scaffold protein , iron–sulfur cluster , mitochondrion , mutant , biochemistry , chemistry , iron binding proteins , microbiology and biotechnology , yeast , biology , enzyme , gene , aconitase , signal transduction
Friedreich's ataxia is caused by a deficit in the mitochondrial protein frataxin. The present work demonstrates that in vivo yeast frataxin Yfh1p and Isu1p, the mitochondrial scaffold protein for the Fe–S cluster assembly, have tightly linked biological functions, acting in concert to promote the Fe–S cluster assembly. A synthetic lethal screen on high iron media with the mild G107D yfh1 mutant has specifically identified Isu1p. Analysis of the cellular phenotypes resulting from pairwise combinations of yfh1 and isu1 mutations, and cross‐linking experiments in isolated mitochondria provide evidence for a direct interaction between Yfh1p and Isu1p.