Journal
MOLECULAR PLANT
Volume 5, Issue 5, Pages 1001-1010Publisher
CELL PRESS
DOI: 10.1093/mp/sss037
Keywords
cysteine desulfurase; Fe-S biogenesis; mitochondria; Arabidopsis; frataxin
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Funding
- ANPCyT [PICT 00614, 0729]
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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 V-max and decreasing the S-0.5 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.
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