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Acylated plastoquinone is a novel neutral lipid accumulated in cyanobacteria.
- Source :
-
PNAS nexus [PNAS Nexus] 2023 Mar 22; Vol. 2 (5), pp. pgad092. Date of Electronic Publication: 2023 Mar 22 (Print Publication: 2023). - Publication Year :
- 2023
-
Abstract
- Although cyanobacteria do not possess bacterial triacylglycerol (TAG)-synthesizing enzymes, the accumulation of TAGs and/or lipid droplets has been repeatedly reported in a wide range of species. In most cases, the identification of TAG has been based on the detection of the spot showing the mobility similar to the TAG standard in thin-layer chromatography (TLC) of neutral lipids. In this study, we identified monoacyl plastoquinol (acyl PQH) as the predominant molecular species in the TAG-like spot from the unicellular Synechocystis sp. PCC 6803 ( S .6803) as well as the filamentous Nostocales sp., Nostoc punctiforme PCC 73102, and Anabaena sp. PCC 7120. In S .6803, the accumulation level of acyl PQH but not TAG was affected by deletion or overexpression of slr2103 , indicating that acyl PQH is the physiological product of Slr2103 having homology with the eukaryotic diacylglycerol acyltransferase-2 (DGAT2). Electron microscopy revealed that cyanobacterial strains used in this study do not accumulate lipid droplet structures such as those observed in oleaginous microorganisms. Instead, they accumulate polyhydroxybutyrate (PHB) granules and/or aggregates of alkane, free C16 and C18 saturated fatty acids, and low amounts of TAG in the cytoplasmic area, which can be detected by staining with a fluorescent dye specific to neutral lipids. Unlike these lipophilic materials, acyl PQH is exclusively localized in the membrane fraction. There must be DGAT2-like enzymatic activity esterifying de novo-synthesized C16 and C18 fatty acids to PQH <subscript>2</subscript> in the thylakoid membranes.<br /> (© The Author(s) 2023. Published by Oxford University Press on behalf of National Academy of Sciences.)
Details
- Language :
- English
- ISSN :
- 2752-6542
- Volume :
- 2
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- PNAS nexus
- Publication Type :
- Academic Journal
- Accession number :
- 37152674
- Full Text :
- https://doi.org/10.1093/pnasnexus/pgad092