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Phosphorylation of Phosphoenolpyruvate Carboxylase Is Essential for Maximal and Sustained Dark CO2 Fixation and Core Circadian Clock Operation in the Obligate Crassulacean Acid Metabolism Species Kalanchoë fedtschenkoi

Boxall, Susanna F. ; Dever, Louisa V. ; Kneřová, Jana ; Gould, Peter D. ; Hartwell, James

The Plant cell, 2017-10, Vol.29 (10), p.2519-2536 [Periódico revisado por pares]

Rockville: American Society of Plant Biologists

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  • Título:
    Phosphorylation of Phosphoenolpyruvate Carboxylase Is Essential for Maximal and Sustained Dark CO2 Fixation and Core Circadian Clock Operation in the Obligate Crassulacean Acid Metabolism Species Kalanchoë fedtschenkoi
  • Autor: Boxall, Susanna F. ; Dever, Louisa V. ; Kneřová, Jana ; Gould, Peter D. ; Hartwell, James
  • Assuntos: Abundance ; Accumulation ; Acids ; Arrhythmia ; Biological clocks ; Carbon dioxide ; Carbon dioxide fixation ; Carbon sequestration ; Circadian rhythm ; Circadian rhythms ; Core loss ; Crassulacean acid metabolism ; Feedback inhibition ; Kalanchoe fedtschenkoi ; Kinases ; Malate ; Metabolism ; Oscillations ; Phosphoenolpyruvate carboxylase ; Phosphorylation ; Protein kinase ; Protein kinase C ; RNA-mediated interference ; Species ; Starch ; Transcription
  • É parte de: The Plant cell, 2017-10, Vol.29 (10), p.2519-2536
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
    SC0008834
    USDOE
    www.plantcell.org/cgi/doi/10.1105/tpc.17.00301
    Current address: Department of Plant Sciences, Downing Street, University of Cambridge, Cambridge CB2 3EA, UK.
    The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantcell.org) is: James Hartwell (james.hartwell@liverpool.ac.uk).
  • Descrição: Phosphoenolpyruvate carboxylase (PPC; EC 4.1.1.31) catalyzes primary nocturnal CO2 fixation in Crassulacean acid metabolism (CAM) species. CAM PPC is regulated posttranslationally by a circadian clock-controlled protein kinase called phosphoenolpyruvate carboxylase kinase (PPCK). PPCK phosphorylates PPC during the dark period, reducing its sensitivity to feedback inhibition by malate and thus enhancing nocturnal CO2 fixation to stored malate. Here, we report the generation and characterization of transgenic RNAi lines of the obligate CAM species Kalanchoë fedtschenkoi with reduced levels of KfPPCK1 transcripts. Plants with reduced or no detectable dark phosphorylation of PPC displayed up to a 66% reduction in total dark period CO2 fixation. These perturbations paralleled reduced malate accumulation at dawn and decreased nocturnal starch turnover. Loss of oscillations in the transcript abundance of KfPPCK1 was accompanied by a loss of oscillations in the transcript abundance of many core circadian clock genes, suggesting that perturbing the only known link between CAM and the circadian clock feeds back to perturb the central circadian clock itself. This work shows that clock control of KfPPCK1 prolongs the activity of PPC throughout the dark period in K. fedtschenkoi, optimizing CAM-associated dark CO2 fixation, malate accumulation, CAM productivity, and core circadian clock robustness.
  • Editor: Rockville: American Society of Plant Biologists
  • Idioma: Inglês
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