title: Loss of the Atypical Kinases ABC1K7 and ABC1K8 Changes the Lipid Composition of the Chloroplast Membrane.
abstract: The activity of bc1 complex kinase (ABC1K) family is a large group of atypical protein kinases found in prokaryotes and eukaryotes. In bacteria and mitochondria, ABC1K kinases are necessary for the synthesis of coenzyme Q and are therefore involved in the respiratory pathway. In chloroplasts, they are involved in prenylquinone synthesis and stress responses, but their functional role remains unclear. Plants can respond to biotic and abiotic stress by modifying membrane fluidity in order to create a suitable environment for the activity of integral membrane proteins. Therefore, this work was focused on the analysis of the effect of ABC1K7 and ABC1K8 on the production of polar lipids and their accumulation in Arabidopsis thaliana leaves. A comparison of abc1k7 and abc1k8 single mutants and the abc1k7/abc1k8 double mutant with wild-type plants and transgenic lines overexpressing ABC1K7 and ABC1K8 was performed using untargeted lipidomic analysis based on liquid chromatography coupled to mass spectrometry. Multivariate data analysis identified sets of chloroplast lipids representing the different genotypes. The abc1k7 and abc1k8 single mutants produced lower levels of the highly unsaturated lipid digalactosyldiacylglycerol (DGDG) than wild-type plants and also different forms of monogalactosyldiacylglycerol (MGDG) and kaempferol. The abc1k8 mutant also produced higher levels of oxylipin-conjugated DGDG and sinapates. The double mutant produced even higher levels of oxylipin-conjugated MGDG and DGDG. These results show that ABC1K7 and ABC1K8 influence chloroplast lipid synthesis or accumulation and modulate chloroplast membrane composition in response to stress.
authors: Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy These authors contributed equally to this work.
authors: Anna
authors: A
authors: Manara
authors: Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy These authors contributed equally to this work.
authors: Giovanni
authors: G
authors: DalCorso
authors: Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy.
authors: Flavia
authors: F
authors: Guzzo
authors: Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy antonella.furini@univr.it.
authors: Antonella
authors: A
authors: Furini
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D015415:Biomarkers / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D002853:Chromatography, Liquid; D016002:Discriminant Analysis; D018506:Gene Expression Regulation, Plant; D007425:Intracellular Membranes / Q000378:metabolism*; D016018:Least-Squares Analysis; D050356:Lipid Metabolism / Q000235:genetics; D013058:Mass Spectrometry; D055442:Metabolome; D055432:Metabolomics; D009154:Mutation / Q000235:genetics; D018515:Plant Leaves / Q000378:metabolism; D025341:Principal Component Analysis; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D060888:Real-Time Polymerase Chain Reaction; D059467:Transcriptome / Q000235:genetics
chemical_list: D029681:Arabidopsis Proteins; D015415:Biomarkers; C000605521:ABC1K7 protein, Arabidopsis; C000605522:ABC1K8 protein, Arabidopsis; D011494:Protein Kinases
keywords: ABC1K proteins; ABC1K7; ABC1K8; Galactolipids; Lipidomics; Oxylipins