TY - JOUR
T1 - An ancient metabolite damage-repair system sustains photosynthesis in plants
AU - Leister, Dario
AU - Sharma, Anurag
AU - Kerber, Natalia
AU - Nägele, Thomas
AU - Reiter, Bennet
AU - Pasch, Viviana
AU - Beeh, Simon
AU - Jahns, Peter
AU - BARBATO, Roberto
AU - Pribil, Mathias
AU - Rühle, Thilo
PY - 2023
Y1 - 2023
N2 - Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major catalyst in the conversion of carbon dioxide into organic compounds in photosynthetic organisms. However, its activity is impaired by binding of inhibitory sugars such as xylulose-1,5-bisphosphate (XuBP), which must be detached from the active sites by Rubisco activase. Here, we show that loss of two phosphatases in Arabidopsis thaliana has detrimental effects on plant growth and photosynthesis and that this effect could be reversed by introducing the XuBP phosphatase from Rhodobacter sphaeroides. Biochemical analyses revealed that the plant enzymes specifically dephosphorylate XuBP, thus allowing xylulose-5-phosphate to enter the Calvin-Benson-Bassham cycle. Our findings demonstrate the physiological importance of an ancient metabolite damage-repair system in degradation of by-products of Rubisco, and will impact efforts to optimize carbon fixation in photosynthetic organisms.
Rubisco is responsible for sequestering virtually all of the carbon dioxide in the global carbon cycle. Here, the authors demonstrate that two conserved phosphatases degrade Rubisco misfire products that inhibit photosynthesis in plants.
AB - Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major catalyst in the conversion of carbon dioxide into organic compounds in photosynthetic organisms. However, its activity is impaired by binding of inhibitory sugars such as xylulose-1,5-bisphosphate (XuBP), which must be detached from the active sites by Rubisco activase. Here, we show that loss of two phosphatases in Arabidopsis thaliana has detrimental effects on plant growth and photosynthesis and that this effect could be reversed by introducing the XuBP phosphatase from Rhodobacter sphaeroides. Biochemical analyses revealed that the plant enzymes specifically dephosphorylate XuBP, thus allowing xylulose-5-phosphate to enter the Calvin-Benson-Bassham cycle. Our findings demonstrate the physiological importance of an ancient metabolite damage-repair system in degradation of by-products of Rubisco, and will impact efforts to optimize carbon fixation in photosynthetic organisms.
Rubisco is responsible for sequestering virtually all of the carbon dioxide in the global carbon cycle. Here, the authors demonstrate that two conserved phosphatases degrade Rubisco misfire products that inhibit photosynthesis in plants.
UR - https://iris.uniupo.it/handle/11579/170323
U2 - 10.1038/s41467-023-38804-y
DO - 10.1038/s41467-023-38804-y
M3 - Article
SN - 2041-1723
VL - 14
JO - Nature Communications
JF - Nature Communications
IS - 1
ER -