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Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana ,
Author(s) -
Busi Maria V.,
Zabaleta Eduardo J.,
Araya Alejandro,
Gomez-Casati Diego F.
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/j.febslet.2004.09.003
Subject(s) - frataxin , complementation , biology , mutant , arabidopsis , gene , biochemistry , nuclear gene , saccharomyces cerevisiae , arabidopsis thaliana , iron binding proteins , mitochondrion , microbiology and biotechnology , genetics , mitochondrial dna
Frataxin is a highly conserved protein from bacteria to mammals that has been proposed to participate in iron–sulfur cluster assembly and mitochondrial iron homeostasis. In higher organisms, the frataxin gene is nuclear‐encoded and the protein is required for maintenance of normal mitochondrial iron levels and respiration. We describe here AtFH , a plant gene with significant homology to other members of the frataxin family. Plant frataxin has five segments of beta regions and two alpha helices, which are characteristics of human frataxin, as well as a potential N‐terminal targeting peptide for the mitochondrial localization. Transcription analysis showed that AtFH is ubiquitously expressed with high levels in flowers. Complementation of a Saccharomyces cerevisiae mutant (Δ yfh ) lacking the frataxin gene proved that AtFH is a functional protein, because it restored normal rates of respiration, growth and sensitivity to H 2 O 2 of the null mutant. Our results support the involvement of AtFH in mitochondrial respiration and survival during oxidative stress in plants. This is the first report of a functional frataxin gene in plants.