ATM1, an essential conserved transporter in Apicomplexa, bridges mitochondrial and cytosolic [Fe-S] biogenesis - Addition
This dataset is an addition to another deposition: https://doi.org/10.26037/yareta:imf7o2y5kvghzefwecqsemjh3y It includes proteomics data of cells overexpressing a second copy of TgATM1 in the UPRT locus in addition to TgATM1 in the endogenous locus. This data complements that of cells depleted in TgATM1 - see above URL. All information is provided in the included file and the associated publication. The Apicomplexa phylum encompasses numerous obligate intracellular parasites with severe implications for human health, including Plasmodium, Cryptosporidium, and Toxoplasma gondii. The iron-sulfur cluster [Fe-S] biogenesis, ISC pathway, localized within the mitochondrion or mitosome of these parasites, is vital for parasite survival and development. Previous work on T. gondii provided insights into the mechanisms of [Fe-S] biogenesis within this phylum, although the transporter linking mitochondria-generated [Fe-S] with cytosolic [Fe-S] assembly (CIA) pathway remained elusive. This critical step is catalysed by a well-conserved ABC transporter in numerous species, termed ATM1 in yeast, ATM3 in plants and ABCB7 in mammals. Here we uncover PfATM1 and TgATM1 and demonstrate its role in transporting [Fe-S] across apicomplexan parasite mitochondrial membranes. While downregulation of TgATM1 does not specifically affect mitochondrial metabolism, it impacts on [Fe-S] protein levels, indicating its role in cellular homeostasis. Depletion of TgATM1 can be complemented through expression of the well-characterized yeast homologue, ScATM1, further validating the function of the apicomplexan transporter. PfATM1's biochemical characterization shows interactions with mitochondrial ISC proteins and the cytosolic CIA protein PfNBP35, confirming it as a functional ABC transporter, modulated by oxidized glutathione (GSSG) and [4Fe-4S].
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- DSF Lab
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- Apicomplexa, Toxoplasma gondii, Plasmodium falciparum, ABC transporter, Mitochondrion, [Fe-S], ATM1, CIA pathway, Proteomics
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- Abboud, Ernest
- Kloehn, Joachim
- Soldati-Favre, Dominique
- Habib, Saman
- Shrivastava, Deepti
- Prasad, Jadhav
- Jha, Akanksha
- Chaurasia, Animesh
- Mitra, Kalyan
- Sadik, Mohammad
- Siddiqi, MI
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