Salt stress increases the Ca2+-independent phosphoenolpyruvate carboxylase kinase activity in Sorghum leaves

Planta. 2001 Dec;214(2):283-7. doi: 10.1007/s004250100616.

Abstract

In C4 plants, the photosynthetic enzyme phosphoenolpyruvate carboxylase (PEPCase; EC 4.1.1.31) is subjected to a phosphorylation process via the light-dependent up-regulation of a Ca2+-independent PEPCase-kinase. The present work aimed to study the effect of salt stress on PEPCase phosphorylation in Sorghum vulgare Pers. leaves. The growth of salt-treated plants was reduced compared with that of the control plants. PEPCase activity modestly increased (around 20-40%) whereas PEPCase phosphorylation was markedly enhanced, on a protein basis, in extracts from illuminated leaves. The enhanced protein kinase activity was found to display a low molecular mass in the range 32-35 kDa, to be independent of Ca2+ and to be up-regulated by light. Furthermore, up-regulation was blocked in vivo by the cytosolic protein synthesis inhibitor cycloheximide. Collectively, these data demonstrated that salinity stress altered the Ca2+-independent PEPCase-kinase, presumably by increasing the mesophyll content of the enzyme. Potassium chloride, but not abscisic acid, mimicked the effect of NaCl on PEPCase-kinase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Abscisic Acid / pharmacology*
  • Calcium / metabolism
  • Light
  • Phosphorylation
  • Photosynthesis / physiology
  • Plant Growth Regulators / pharmacology*
  • Plant Leaves / drug effects
  • Plant Leaves / enzymology*
  • Plant Leaves / growth & development
  • Poaceae / drug effects
  • Poaceae / enzymology*
  • Poaceae / growth & development
  • Protein Serine-Threonine Kinases / metabolism*
  • Sodium Chloride / pharmacology*
  • Up-Regulation

Substances

  • Plant Growth Regulators
  • Sodium Chloride
  • Abscisic Acid
  • phosphoenolpyruvate carboxylase kinase
  • Protein Serine-Threonine Kinases
  • Calcium