ArticleThe Journal of biological chemistry2022
Deciphering functional redundancy and energetics of malate oxidation in mycobacteria.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 26 citations in OpenAlex.
- An adenylyl cyclase switch reroutes carbon from growth to virulence lipids inbioRxiv : the preprint server for biology · 2026Article
- Dual inhibition of respiratory complexes inMicrobiology spectrum · 2026Article
- AscF in the mycobacterial CIII-CIV supercomplex lacks metal and nucleotide binding but links malate oxidation to respiration.FEBS letters · 2026Article
- Structural basis for EtfD-mediated coupling of β-oxidation and the respiratory chain in mycobacteria.The EMBO journal · 2026Article
- Physiological, genetical and morphological alterations in Mycobacterium avium subsp. paratuberculosis mutants generated with the CRISPRi system.BMC microbiology · 2026Article
- Article
- Protective Effect of Lycium Barbarum Polysaccharides and Sodium Selenite on Cadmium Chloride-Induced Testicular Toxicity in Rats.Biological trace element research · 2025Article
- Functional analysis of the intracellular survival ofJournal of bacteriology · 2025Article
- Cryo-EM of native membranes reveals an intimate connection between the Krebs cycle and aerobic respiration in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Wastewater Treatment with Bacterial Representatives of theInternational journal of molecular sciences · 2024Review
- High-throughput functional genomics: A (myco)bacterial perspective.Molecular microbiology · 2023Review
- Mechanism of mycobacterial ATP synthase inhibition by squaramides and second generation diarylquinolines.The EMBO journal · 2023Article
- Biochemical characterization and identification of ferulenol and embelin as potent inhibitors of malate:quinone oxidoreductase fromFrontiers in molecular biosciences · 2023Article
- Supplementation of Dietary Crude Lentinan Improves the Intestinal Microbiota and Immune Barrier in Rainbow Trout (Frontiers in immunology · 2022Article
- Succinyl-CoA:acetate CoA-transferase functioning in the oxidative tricarboxylic acid cycle inFrontiers in microbiology · 2022Article
- Uncovering interactions between mycobacterial respiratory complexes to target drug-resistantFrontiers in cellular and infection microbiology · 2022Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oxidation of malate to oxaloacetate, catalyzed by either malate dehydrogenase (Mdh) or malate quinone oxidoreductase (Mqo), is a critical step of the tricarboxylic acid cycle. Both Mqo and Mdh are found in most bacterial genomes, but the level of functional redundancy between these enzymes remains unclear. A bioinformatic survey revealed that Mqo was not as widespread as Mdh in bacteria but that it was highly conserved in mycobacteria. We therefore used mycobacteria as a model genera to study the functional role(s) of Mqo and its redundancy with Mdh. We deleted mqo from the environmental saprophyte Mycobacterium smegmatis, which lacks Mdh, and found that Mqo was essential for growth on nonfermentable carbon sources. On fermentable carbon sources, the Δmqo mutant exhibited delayed growth and lowered oxygen consumption and secreted malate and fumarate as terminal end products. Furthermore, heterologous expression of Mdh from the pathogenic species Mycobacterium tuberculosis shortened the delayed growth on fermentable carbon sources and restored growth on nonfermentable carbon sources at a reduced growth rate. In M. tuberculosis, CRISPR interference of either mdh or mqo expression resulted in a slower growth rate compared to controls, which was further inhibited when both genes were knocked down simultaneously. These data reveal that exergonic Mqo activity powers mycobacterial growth under nonenergy limiting conditions and that endergonic Mdh activity complements Mqo activity, but at an energetic cost for mycobacterial growth. We propose Mdh is maintained in slow-growing mycobacterial pathogens for use under conditions such as hypoxia that require reductive tricarboxylic acid cycle activity.
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