Iron-sulfur cluster complex assembly in the mitochondria of Arabidopsis thaliana.

TERENZI, AGUSTINA; DIEGO FABIAN GOMEZ CASATI; TERENZI, AGUSTINA; DIEGO FABIAN GOMEZ CASATI; BALPARDA, MANUEL; PAGANI, MARIA A.; BALPARDA, MANUEL; PAGANI, MARIA A.; ARMAS, ALEJANDRO M.; BUSI, MARIA VICTORIA; ARMAS, ALEJANDRO M.; BUSI, MARIA VICTORIA

Plants

MDPI

Año: 2020 vol. 9

2223-7747

In plants, the cysteine desulfurase (AtNFS1) and frataxin (AtFH) are involved in theformation of Fe-S groups in mitochondria, specifically, in Fe and sulfur loading onto scaold proteins, and the subsequent formation of the mature Fe-S cluster. We found that the small mitochondrial chaperone, AtISD11, and AtFH are positive regulators for AtNFS1 activity in Arabidopsis. Moreover, when the three proteins were incubated together, a stronger attenuation of the Fenton reaction was observed compared to that observed with AtFH alone. Using pull-down assays, we found that these three proteins physically interact, and sequence alignment and docking studies showed that several amino acid residues reported as critical for the interaction of their human homologous are conserved. Our results suggest that AtFH, AtNFS1 and AtISD11 form a multiprotein complex that could be involved in dierent stages of the iron?sulfur cluster (ISC) pathway in plant mitochondria.