In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase AtPPC1 in phosphate-starved Arabidopsis thaliana.

ABSTRACT: PEPC [PEP(phosphoenolpyruvate) carboxylase] is a tightly controlled cytosolic enzyme situated at a major branchpoint in plant metabolism. Accumulating evidence indicates important functions for PEPC and PPCK (PEPC kinase) in plant acclimation to nutritional P(i) deprivation. However, little is known about the genetic origin or phosphorylation status of native PEPCs from -P(i) (P(i)-deficient) plants. The transfer of Arabidopsis suspension cells or seedlings to -P(i) growth media resulted in: (i) the marked transcriptional upregulation of genes encoding the PEPC isoenzyme AtPPC1 (Arabidopsis thaliana PEPC1), and PPCK isoenzymes AtPPCK1 and AtPPCK2; (ii) >2-fold increases in PEPC specific activity and in the amount of an immunoreactive 107-kDa PEPC polypeptide (p107); and (iii) In vivo p107

SUBMITTER: Gregory AL 

PROVIDER: S-EPMC2677216 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature