Artículos de revistas
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana
Fecha
2012-09Registro en:
Turowski, Valeria Rosana; Busi, María Victoria; Gomez Casati, Diego Fabian; Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana; Oxford University Press; Molecular Plant; 5; 5; 9-2012; 1001-1010
1674-2052
Autor
Turowski, Valeria Rosana
Busi, María Victoria
Gomez Casati, Diego Fabian
Resumen
AtNfs1 is the Arabidopsis thaliana mitochondrial homolog of the bacterial cysteine desulfurases NifS and IscS, having an essential role in cellular Fe–S cluster assembly. Homology modeling of AtNfs1m predicts a high global similarity with E. coli IscS showing a full conservation of residues involved in the catalytic site, whereas the chloroplastic AtNfs2 is more similar to the Synechocystis sp. SufS. Pull-down assays showed that the recombinant mature form, AtNfs1m, specifically binds to Arabidopsis frataxin (AtFH). A hysteretic behavior, with a lag phase of several minutes, was observed and hysteretic parameters were affected by pre-incubation with AtFH. Moreover, AtFH modulates AtNfs1m kinetics, increasing Vmax and decreasing the S0.5 value for cysteine. Results suggest that AtFH plays an important role in the early steps of Fe–S cluster formation by regulating AtNfs1 activity in plant mitochondria.