The two divergent PEP-carboxylase catalytic subunits in the green microalga Chlamydomonas reinhardtii respond reversibly to inorganic-N supply and co-exist in the high-molecular-mass, hetero-oligomeric Class-2 PEPC complex

FEBS Lett. 2007 Oct 16;581(25):4871-6. doi: 10.1016/j.febslet.2007.09.015. Epub 2007 Sep 17.

Abstract

Our recent molecular studies revealed two divergent PEP-carboxylase (PEPC [Ppc]) encoding genes in the green microalga Chlamydomonas reinhardtii, CrPpc1 and CrPpc2, which are coordinately responsive to changes in inorganic-N and -C supply at the transcript level [Mamedov, T.G., Moellering, E.R. and Chollet, R. (2005) Identification and expression analysis of two inorganic C- and N-responsive genes encoding novel and distinct molecular forms of eukaryotic phosphoenolpyruvate carboxylase in the green microalga C. reinhardtii, Plant J. 42, 832-843]. Here, we report the distribution of these two encoded catalytic subunits in the minor Class-1 and predominant Class-2 PEPC enzyme-forms, the latter of which is a novel high-molecular-mass, hetero-oligomeric complex containing both CrPpc1 (p109) and CrPpc2 (p131) polypeptides. The Class-1 enzyme, however, is a typical PEPC homotetramer comprised solely of p109. We also document that the amount of both CrPpc1/2 catalytic subunits is up-/down-regulated by varying levels of NH(4)(+) supplied to the culture medium.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Algal Proteins / chemistry
  • Algal Proteins / immunology
  • Algal Proteins / metabolism*
  • Animals
  • Antibody Specificity
  • Catalytic Domain
  • Chlamydomonas reinhardtii / enzymology*
  • Culture Media
  • Electrophoresis, Gel, Two-Dimensional
  • Electrophoresis, Polyacrylamide Gel
  • Immunoblotting
  • Phosphoenolpyruvate Carboxylase / chemistry
  • Phosphoenolpyruvate Carboxylase / immunology
  • Phosphoenolpyruvate Carboxylase / metabolism*
  • Protein Denaturation
  • Protein Subunits / chemistry
  • Protein Subunits / immunology
  • Protein Subunits / metabolism
  • Quaternary Ammonium Compounds / metabolism
  • Zea mays / enzymology

Substances

  • Algal Proteins
  • Culture Media
  • Protein Subunits
  • Quaternary Ammonium Compounds
  • Phosphoenolpyruvate Carboxylase