INVESTIGADORES
ZABALETA Eduardo Julian
congresos y reuniones científicas
Título:
MOLECULAR CLONING, EXPRESSION AND PURIFICATION OF Arabidopdid thaliana Frataxin Homolog (AtFH)
Autor/es:
MALIANDI, M. V.; VALDEZ, H.; BUSI, V.; EDUARDO JULIAN ZABALETA; ARAYA, A; GÓMEZ-CASATI, D.
Lugar:
Pinamar
Reunión:
Congreso; PABMB 10th congress; 2005
Resumen:
It has been proposed that frataxin, a nuclear encoded mitochondrial
protein, participates in Fe-S cluster assembly, mitochondrial energy
metabolism, respiration and iron homeostasis, but its precise
function remains elusive. This protein is highly conserved from
bacteria to mammals and plants without major structural changes,
specially at the C-terminal domain, suggesting that it could play
similar function in all these organisms. We recently described AtFH,
a plant gene with significant homology to other members of the
frataxin family. The plant frataxin domain was expressed inAtFH,
a plant gene with significant homology to other members of the
frataxin family. The plant frataxin domain was expressed in
Escherichia coli BL21-CodonPlus (DE3)-RIL cells and purified by
one-step Ni-chelating chromatography. The protein was determined
to be 98% pure and migrates as a single protein band of about 15
kDa as assessed by SDS-PAGE. Arabidopsis null mutants deficient
in AtFH expression showed higher rate of CO2 fixation respect to
wt. Results also showed that this protein is escential for full-activity
of succinate dehydrogenase (SDH) and aconitase, two mitochondrial
iron-sulphur containing enzymes.
Results are in agreement with the involvement of AtFH in Fe-S
cluster assembly in plant mitochondria.BL21-CodonPlus (DE3)-RIL cells and purified by
one-step Ni-chelating chromatography. The protein was determined
to be 98% pure and migrates as a single protein band of about 15
kDa as assessed by SDS-PAGE. Arabidopsis null mutants deficient
in AtFH expression showed higher rate of CO2 fixation respect to
wt. Results also showed that this protein is escential for full-activity
of succinate dehydrogenase (SDH) and aconitase, two mitochondrial
iron-sulphur containing enzymes.
Results are in agreement with the involvement of AtFH in Fe-S
cluster assembly in plant mitochondria.Arabidopsis null mutants deficient
in AtFH expression showed higher rate of CO2 fixation respect to
wt. Results also showed that this protein is escential for full-activity
of succinate dehydrogenase (SDH) and aconitase, two mitochondrial
iron-sulphur containing enzymes.
Results are in agreement with the involvement of AtFH in Fe-S
cluster assembly in plant mitochondria.2 fixation respect to
wt. Results also showed that this protein is escential for full-activity
of succinate dehydrogenase (SDH) and aconitase, two mitochondrial
iron-sulphur containing enzymes.
Results are in agreement with the involvement of AtFH in Fe-S
cluster assembly in plant mitochondria.