ArticleMolecular microbiology2017
A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species.
Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- 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
- The mitochondrion ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Interplay between Yersinia pestis and its flea vector in lipoate metabolism.The ISME journal · 2021Article
- 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
- Dynamic Relay of Protein-Bound Lipoic Acid in Staphylococcus aureus.Journal of bacteriology · 2019Article
- Article
- Development and retention of a primordial moonlighting pathway of protein modification in the absence of selection presents a puzzle.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.Proteins · 2017Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Lipoate is an essential cofactor for enzymes that are important for central metabolism and other processes. In malaria parasites, scavenged lipoate from the human host is required for survival. The Plasmodium falciparum mitochondrion contains two enzymes (PfLipL1 and PfLipL2) that are responsible for activating mitochondrial proteins through the covalent attachment of lipoate (lipoylation). Lipoylation occurs via a novel redox-gated mechanism that remains poorly understood. We show that PfLipL1 functions as a redox switch that determines which downstream proteins will be activated. Based on the lipoate redox state, PfLipL1 either functions as a canonical lipoate ligase or as a lipoate activating enzyme which works in conjunction with PfLipL2. We demonstrate that PfLipL2 is a lipoyltransferase and is a member of a novel clade of lipoate attachment enzymes. We show that a LipL2 enzyme from Chlamydia trachomatis has similar activity, demonstrating conservation between intracellular pathogens from different phylogenetic kingdoms and supporting the hypothesis that an early ancestor of malaria parasites once contained a chlamydial endosymbiont. Redox-dependent lipoylation may regulate processes such as central metabolism and oxidative defense pathways.
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Registered trials
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