Frataxin Oligomerization and metal binding properties in plants.

BUCHENSKY, C.; SANCHEZ, M.; CAPDEVILA, M.; DOMINGUEZ VERA, J; ATRIAN, S.; PAGANI M.A.; BUSI, M. V.; DIEGO FABIAN GOMEZ CASATI

Córdoba

Congreso; LII Reunión de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB); 2016

SAIB

Frataxinis a highly conserved protein involved in Fe-S cluster biosynthesis, ironhomeostasis, heme metabolism and protection against oxidative damage. Inhumans, defects in frataxin levels lead to Friedreich's ataxia, a progressive neurodegenerativediseasePrevious studies in E. coli, S. cerevisiae and human frataxinindicate that these proteins present different oligomerization behavior anddifferent metals binding properties, which are specific to each species. Also,it has been reported that the N-terminal transit sequence that directs itstransport to the mitochondria participates in these processes. In plants,frataxin is found in both chloroplast and mitochondria.Inthe present work, we characterized A.thaliana (AtFH) and Zea mays(ZmFH1 and ZmFH2) frataxin proteins. Recombinant proteins in full length, in anintermediate form and in mature form without transit peptide were synthesized,and then they were studied by ESI-MS spectroscopy. Results indicate thatfrataxins from both plants present common oligomerization and metals bindingproperties. In addition, we determined that the N-terminal region is importantin these processes, and our findings suggest the existence of self cleavage toreach the mature form.