ArticleJournal of bacteriology2009
Deletion of citrate synthase restores growth of Sinorhizobium meliloti 1021 aconitase mutants.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Deletion ofApplied and environmental microbiology · 2025Article
- Interaction and Regulation of Carbon, Nitrogen, and Phosphorus Metabolisms in Root Nodules of Legumes.Frontiers in plant science · 2018Review
- Role of O2 in the Growth of Rhizobium leguminosarum bv. viciae 3841 on Glucose and Succinate.Journal of bacteriology · 2017Article
- Secreted Citrate Serves as Iron Carrier for the Marine PathogenFrontiers in cellular and infection microbiology · 2017Article
- Lipogenesis and Redox Balance in Nitrogen-Fixing Pea Bacteroids.Journal of bacteriology · 2016Article
- Oxidative metabolism enables Salmonella evasion of the NLRP3 inflammasome.The Journal of experimental medicine · 2014Article
- Two roles for aconitase in the regulation of tricarboxylic acid branch gene expression in Bacillus subtilis.Journal of bacteriology · 2013Article
- Deletion of the aconitase gene in Corynebacterium glutamicum causes strong selection pressure for secondary mutations inactivating citrate synthase.Journal of bacteriology · 2011Article
- Large scale physiological readjustment during growth enables rapid, comprehensive and inexpensive systems analysis.BMC systems biology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The symbiotic nitrogen-fixing bacterium Sinorhizobium meliloti 1021 encodes only one predicted aconitase (AcnA) in its genome. AcnA has a significant degree of similarity with other bacterial aconitases that behave as dual proteins: enzymes and posttranscriptional regulators of gene expression. Similar to the case with these bacterial aconitases, AcnA activity was reversibly labile and was regained upon reconstitution with reduced iron. The aconitase promoter was active in root nodules. acnA mutants grew very poorly, had secondary mutations, and were quickly outgrown by pseudorevertants. The acnA gene was stably interrupted in a citrate synthase (gltA) null background, indicating that the intracellular accumulation of citrate may be deleterious for survival of strain 1021. No aconitase activity was detected in this mutant, suggesting that the acnA gene encodes the only functional aconitase of strain 1021. To uncover a function of AcnA beyond its catalytic role in the tricarboxylic acid cycle pathway, the gltA acnA double mutant was compared with the gltA single mutant for differences in motility, resistance to oxidative stress, nodulation, and growth on different substrates. However, no differences in any of these characteristics were found.
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