ArticleMolecular microbiology2014
Redox-dependent lipoylation of mitochondrial proteins in Plasmodium falciparum.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Staphylococcus aureus exploits lipoic acid salvage to combat host oxidative stress.Cell reports · 2025Article
- Lipoic acid attachment to proteins: stimulating new developments.Microbiology and molecular biology reviews : MMBR · 2024Review
- Substrate Analogues Entering the Lipoic Acid Salvage Pathway via Lipoate-Protein Ligase 2 Interfere withACS infectious diseases · 2024Article
- A Chemical Proteomic Strategy Reveals Inhibitors of Lipoate Salvage in Bacteria and Parasites.Angewandte Chemie (International ed. in English) · 2023Article
- The mitochondrion ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The ferredoxin redox system - an essential electron distributing hub in the apicoplast of Apicomplexa.Trends in parasitology · 2022Review
- Lipoic Acid Metabolism as a Potential Chemotherapeutic Target AgainstFrontiers in chemistry · 2021Review
- A Way Forward for Culturing Plasmodium vivax.Trends in parasitology · 2020Review
- A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism inFrontiers in microbiology · 2020Article
- Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inFrontiers in cellular and infection microbiology · 2020Article
- Dynamic Relay of Protein-Bound Lipoic Acid in Staphylococcus aureus.Journal of bacteriology · 2019Article
- Article
- Genomic and transcriptomic alterations in Leishmania donovani lines experimentally resistant to antileishmanial drugs.International journal for parasitology. Drugs and drug resistance · 2018Article
- Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus.Molecular microbiology · 2018Article
- A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species.Molecular microbiology · 2017Article
- Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.Proteins · 2017Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Lipoate scavenging from the human host is essential for malaria parasite survival. Scavenged lipoate is covalently attached to three parasite proteins: the H-protein and the E2 subunits of branched chain amino acid dehydrogenase (BCDH) and α-ketoglutarate dehydrogenase (KDH). We show mitochondrial localization for the E2 subunits of BCDH and KDH, similar to previously localized H-protein, demonstrating that all three lipoylated proteins reside in the parasite mitochondrion. The lipoate ligase 1, LipL1, has been shown to reside in the mitochondrion and it catalyses the lipoylation of the H-protein; however, we show that LipL1 alone cannot lipoylate BCDH or KDH. A second mitochondrial protein with homology to lipoate ligases, LipL2, does not show ligase activity and is not capable of lipoylating any of the mitochondrial substrates. Instead, BCDH and KDH are lipoylated through a novel mechanism requiring both LipL1 and LipL2. This mechanism is sensitive to redox conditions where BCDH and KDH are exclusively lipoylated under strong reducing conditions in contrast to the H-protein which is preferentially lipoylated under less reducing conditions. Thus, malaria parasites contain two different routes of mitochondrial lipoylation, an arrangement that has not been described for any other organism.
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