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• W2007958560 abstract "Surprisingly few protein kinases have been demonstrated in chloroplasts or mitochondria. Here, we discuss the activity of bc1 complex kinase (ABC1K) protein family, which we suggest locate in mitochondria and plastids, thus filling the kinase void. The ABC1Ks are atypical protein kinases and their ancestral function is the regulation of quinone synthesis. ABC1Ks have proliferated from one or two members in non-photosynthetic organisms to more than 16 members in algae and higher plants. In this review, we reconstruct the evolutionary history of the ABC1K family, provide a functional domain analysis for angiosperms and a nomenclature for ABC1Ks in Arabidopsis (Arabidopsis thaliana), rice (Oryza sativa) and maize (Zea mays). Finally, we hypothesize that targets of ABC1Ks include enzymes of prenyl-lipid metabolism as well as components of the organellar gene expression machineries. Surprisingly few protein kinases have been demonstrated in chloroplasts or mitochondria. Here, we discuss the activity of bc1 complex kinase (ABC1K) protein family, which we suggest locate in mitochondria and plastids, thus filling the kinase void. The ABC1Ks are atypical protein kinases and their ancestral function is the regulation of quinone synthesis. ABC1Ks have proliferated from one or two members in non-photosynthetic organisms to more than 16 members in algae and higher plants. In this review, we reconstruct the evolutionary history of the ABC1K family, provide a functional domain analysis for angiosperms and a nomenclature for ABC1Ks in Arabidopsis (Arabidopsis thaliana), rice (Oryza sativa) and maize (Zea mays). Finally, we hypothesize that targets of ABC1Ks include enzymes of prenyl-lipid metabolism as well as components of the organellar gene expression machineries." @default.
• W2007958560 created "2016-06-24" @default.
• W2007958560 creator A5009637778 @default.
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• W2007958560 date "2012-09-01" @default.
• W2007958560 modified "2023-09-26" @default.
• W2007958560 title "ABC1K atypical kinases in plants: filling the organellar kinase void" @default.
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• W2007958560 doi "https://doi.org/10.1016/j.tplants.2012.05.010" @default.
• W2007958560 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3926664" @default.
• W2007958560 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22694836" @default.
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