INVESTIGADORES
GOMEZ CASATI Diego Fabian
congresos y reuniones científicas
Título:
. Characterization of AtNfs1, a mitochondrial cysteine desulphurase from Arabidopsis.
Autor/es:
TUROWSKI, V.; BUSI, M. V.; DIEGO FABIAN GOMEZ CASATI
Lugar:
Carlos Paz, Argentina
Reunión:
Congreso; XLIV Reunión SAIB; 2008
Institución organizadora:
SAIB
Resumen:
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Iron-Sulfur (Fe-S) cluster are ubiquitous prosthetic groups required to sustain fundamental life processes. The assembly of Fe-S clusters requires the coordinated delivery of both iron and sulfide and involves at least ten proteins. The first step in biosynthesis is carried out by cysteine desulfurases (NifS like proteins) which catalyze the formation of elemental sulfur and alanine from cysteine. The Arabidopsis genome encodes two cysteine desulfurases AtNfs1 and AtNfs2. AtNfs2 has been characterized as a plastid protein whereas AtNfs1 has been localized to the mitochondria. In order to characterize this first step in Fe-S cluster biosynthesis in plant mitochondria, we expressed, purified and perform kinetic characterization of the recombinant protein AtNfs1m (lacking the mitochondrial transit peptide). We also examined possible protein interaction of AtNfs1 with the Arabidopsis frataxin homologue, AtFH (a potential donor of iron for the assembly of cluster Fe-S). The results confirmed that AtNfs1m displays cysteine desulfurase activity; moreover, it is possible to speculate that AtFH modulates the activity of AtNfs1.
