Full text is available at the source.
Phosphorylation of Phospho enol pyruvate Carboxylase Is Essential for Maximal and Sustained Dark CO 2 Fixation and Core Circadian Clock Operation in the Obligate Crassulacean Acid Metabolism Species Kalanchoë fedtschenkoi
Phosphorylation of a Key Enzyme Is Needed for Maximum Nighttime CO2 Fixation and Proper Circadian Clock Function in the CAM Plant Kalanchoë fedtschenkoi
AI simplified
Abstract
Plants with reduced dark phosphorylation of phosphopyruvate carboxylase (PPC) exhibited up to a 66% reduction in total dark period CO2 fixation.
- Phosphopyruvate carboxylase kinase (PPCK) regulates PPC by phosphorylating it during the dark period.
- Reduced levels of PPCK led to decreased sensitivity of PPC to feedback inhibition by malate.
- Lower dark phosphorylation of PPC is associated with reduced malate accumulation at dawn.
- A decrease in nocturnal starch turnover was observed alongside the reduced PPC phosphorylation.
- Loss of transcript oscillations for PPCK correlated with disruptions in core circadian clock gene expression.
AI simplified