Phosphoenolpyruvate carboxylase kinase involved in C(4) photosynthesis in Flaveria trinervia: cDNA cloning and characterization

FEBS Lett. 2001 Nov 2;507(3):318-22. doi: 10.1016/s0014-5793(01)02994-5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Asteraceae / enzymology*
  • Asteraceae / genetics
  • Biological Evolution
  • Blotting, Southern
  • Cloning, Molecular
  • Gene Expression Regulation, Plant
  • Molecular Sequence Data
  • Phosphorylation
  • Photosynthesis / physiology
  • Plant Leaves / genetics
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism*
  • Protein-Serine-Threonine Kinases / genetics*
  • Protein-Serine-Threonine Kinases / metabolism*
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Plant Proteins
  • phosphoenolpyruvate carboxylase kinase
  • Protein-Serine-Threonine Kinases

Associated data

  • GENBANK/AB065100