ArticleThe Journal of biological chemistry2009
A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- A bacterial-type cardiolipin synthase in Plasmodium spp. supports mitochondrial respiration and is important for liver stage maturation.PLoS pathogens · 2026Article
- Genomic insights into a novel species, Dyella thailandensis sp. nov., a cellulolytic and xylanolytic bacterium isolated from soil associated with leaf compost.Scientific reports · 2026Article
- Impact of the Deletion of Genes of the Nitrogen Metabolism on Triacylglycerol, Cardiolipin and Actinorhodin Biosynthesis inMicroorganisms · 2024Article
- Mono- to tetra-alkyl ether cardiolipins in a mesophilic, sulfate-reducing bacterium identified by UHPLC-HRMSFrontiers in microbiology · 2024Article
- The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.Extremophiles : life under extreme conditions · 2022Review
- Eugene P. Kennedy's Legacy: Defining Bacterial Phospholipid Pathways and Function.Frontiers in molecular biosciences · 2021Review
- Structure ofCommunications biology · 2019Article
- Disruption of the GDP-mannose synthesis pathway in Streptomyces coelicolor results in antibiotic hyper-susceptible phenotypes.Microbiology (Reading, England) · 2018Article
- Streptomyces coelicolor strains lacking polyprenol phosphate mannose synthase and protein O-mannosyl transferase are hyper-susceptible to multiple antibiotics.Microbiology (Reading, England) · 2018Article
- Cross-species complementation of bacterial- and eukaryotic-type cardiolipin synthases.Microbial cell (Graz, Austria) · 2017Article
- Review
- Elimination of the unnecessary: Intra- and extracellular signaling by anionic phospholipids.Biochemical and biophysical research communications · 2017Review
- Known unknowns of cardiolipin signaling: The best is yet to come.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Molecular species composition of plant cardiolipin determined by liquid chromatography mass spectrometry.Journal of lipid research · 2016Article
- Article
- Plasticity of Streptomyces coelicolor Membrane Composition Under Different Growth Conditions and During Development.Frontiers in microbiology · 2015Article
- The neomuran revolution and phagotrophic origin of eukaryotes and cilia in the light of intracellular coevolution and a revised tree of life.Cold Spring Harbor perspectives in biology · 2014Review
- Structural basis for catalysis in a CDP-alcohol phosphotransferase.Nature communications · 2014Article
- Membrane lipids in Agrobacterium tumefaciens: biosynthetic pathways and importance for pathogenesis.Frontiers in plant science · 2014Review
- Genetics of Capsular Polysaccharides and Cell Envelope (Glyco)lipids.Microbiology spectrum · 2014Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Cardiolipin (CL) is an anionic membrane lipid present in bacteria, plants, and animals, but absent from archaea. It is generally thought that bacteria use an enzyme belonging to the phospholipase D superfamily as cardiolipin synthase (Cls) catalyzing a reversible phosphatidyl group transfer from one phosphatidylglycerol (PG) molecule to another PG to form CL and glycerol. In contrast, in eukaryotes a Cls of the CDP-alcohol phosphatidyltransferase superfamily uses cytidine diphosphate-diacylglycerol (CDP-DAG) as the donor of the phosphatidyl group, which is transferred to a molecule of PG to form CL. Searching the genome of the actinomycete Streptomyces coelicolor A3(2) we identified a gene coding for a putative Cls of the CDP-alcohol phosphatidyltransferase superfamily (Sco1389). Here we show that expression of Sco1389 in a CL-deficient Rhizobium etli mutant restores CL formation. In an in vitro assay Sco1389 condenses CDP-DAG with PG to form CL and therefore catalyzes the same reaction as eukaryotic cardiolipin synthases. This is the first time that a CDP-alcohol phosphatidyltransferase from bacteria is shown to be responsible for CL formation. The broad occurrence of putative orthologues of Sco1389 among the actinobacteria suggests that CL synthesis involving a eukaryotic type Cls is common in actinobacteria.
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