biologia plantarum

Biologia plantarum 49:521-525, 2005 | DOI: 10.1007/s10535-005-0045-2

Heat stress effects on ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco binding protein and Rubisco activase in wheat leaves

K. Demirevska-Kepova^1,*, R. Holzer², L. Simova-Stoilova¹, U. Feller²

¹ Institute of Plant Physiology, Bulgarian Academy of Sciences, Sofia, Bulgaria

² Institute of Plant Science, University of Bern, Bern, Switzerland

Changes in chlorophyll content, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) binding protein (RBP), Rubisco activase (RA), Rubisco large (LS) and small (SS) subunits, and electrolyte leakage were investigated in wheat leaf segments during heat stress (HS) for 1 h and for 24 h at 40 °C in darkness or in light, as well as after recovery from heat stress (HSR) for 24 h at 25 °C in light. The 24-h HS treatment in darkness decreased irreversibly photosynthetic pigments, soluble proteins, RBP, RA, Rubisco LS and SS. An increase in RA and RBP protein contents was observed under 24-h HS and HSR in light. This increase was in accordance with their role as chaperones and the function of RBP as a heat shock protein.

Keywords: high temperature stress; Triticum aestivum L.; immunoblotting

Subjects: chlorophylls, heat stress; electrolyte leakage, heat stress; heat stress, Rubisco; immunoblotting; leakage, electrolyte; protein, soluble, heat stress; ribulose-1,5-bisphosphate carboxylase/oxygenase; Triticum aestivum; wheat, heat stress, rubisco

Received: May 21, 2004; Accepted: April 26, 2005; Published: December 1, 2005  Show citation