Phosphoenolpyruvate carboxylase kinase involved in C(4) photosynthesis in Flaveria trinervia: cDNA cloning and characterization.
In C(4) plants, phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31), a key enzyme in C(4) photosynthesis, is controlled by reversible phosphorylation of a conserved Ser residue near the N-terminus. We now report the first cloning of a cDNA from a C(4) plant, Flaveria trinervia, which encodes the specific protein kinase (FtPEPC-PK) involved in the phosphorylation of C(4)-form PEPC. Several lines of supportive evidence are: strict substrate specificity of the recombinant enzyme, prominent light/dark response of the transcript level and abundant expression in leaves of C(4) plant (F. trinervia) but very low expression in a C(3) plant of the same genus (Flaveria pringlei). We also discuss the possibility that the FtPEPC-PK gene has co-evolved with the PEPC gene to participate in C(4) photosynthesis.
Tsuchida
Y
Y
Laboratory of Plant Physiology, Graduate School of Agriculture, Kyoto University, Japan.
Furumoto
T
T
Izumida
A
A
Hata
S
S
Izui
K
K
D000595:Amino Acid Sequence; D019659:Asteraceae / Q000201:enzymology* / Q000235:genetics; D005075:Biological Evolution; D015139:Blotting, Southern; D003001:Cloning, Molecular; D018506:Gene Expression Regulation, Plant; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010788:Photosynthesis / Q000502:physiology; D018515:Plant Leaves / Q000235:genetics; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D010940:Plant Proteins; C069767:phosphoenolpyruvate carboxylase kinase; D017346:Protein Serine-Threonine Kinases