Premium
Phospho enol pyruvate carboxylase kinase involved in C 4 photosynthesis in Flaveria trinervia : cDNA cloning and characterization 1
Author(s) -
Tsuchida Yuhei,
Furumoto Tsuyoshi,
Izumida Atsushi,
Hata Shingo,
Izui Katsura
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02994-5
Subject(s) - biochemistry , c4 photosynthesis , complementary dna , phosphoenolpyruvate carboxylase , pyruvate carboxylase , biology , photosynthesis , cloning (programming) , phosphorylation , gene , enzyme , computer science , programming language
In C 4 plants, phospho enol pyruvate 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.