Protein-protein interaction studies provide evidence for electron transfer from ferredoxin to lipoic acid synthase in Toxoplasma gondii

FEBS Lett. 2014 Nov 26. pii: S0014-5793(14)00825-4. doi: 10.1016/j.febslet.2014.11.020. [Epub ahead of print]

Frohnecke N1, Klein S1, Seeber F2.

Author information 

Abstract

The only known redox system in the apicoplast, a plastid-like organelle of apicomplexan parasites, is ferredoxin and ferredoxin-associated reductase. Ferredoxin donates electrons to different enzymes, presumably including lipoate synthase (LipA), which is essential for fatty acid biosynthesis. We recombinantly expressed and characterized LipA from the protozoan parasite Toxoplasma gondii, generated LipA-specific antibodies and confirmed the apicoplast localization of LipA. Electron transfer from ferredoxin to LipA would require direct protein-protein interaction. Such a robust interaction between the two proteins was demonstrated in both yeast and bacterial two-hybrid systems. Taken together, our results provide strong evidence for a role of ferredoxin as an electron donor to LipA.

Copyright © 2014. Published by Elsevier B.V.

KEYWORDS: 

Apicomplexa; Ferredoxin; Lipoic acid synthesis; Plastid; Protein interactions; Two-hybrid system

PMID:

 

25433292

 

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