Biologia Plantarum

, Volume 49, Issue 4, pp 521–525

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

  • K. Demirevska-Kepova
  • R. Holzer
  • L. Simova-Stoilova
  • U. Feller

DOI: 10.1007/s10535-005-0045-2

Cite this article as:
Demirevska-Kepova, K., Holzer, R., Simova-Stoilova, L. et al. Biol Plant (2005) 49: 521. doi:10.1007/s10535-005-0045-2


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.

Additional key words

high temperature stressTriticum aestivum L.immunoblotting



electrical conductivity


fresh mass


heat stress


heat shock proteins


recovery after heat stress


Rubisco activase


Rubisco binding protein

Rubisco LS

Rubisco large subunit

Rubisco SS

Rubisco small subunit


ribulose-1,5-bisphosphate carboxylase/oxygenase

Copyright information

© Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Praha 2005

Authors and Affiliations

  • K. Demirevska-Kepova
    • 1
  • R. Holzer
    • 2
  • L. Simova-Stoilova
    • 1
  • U. Feller
    • 2
  1. 1.Institute of Plant PhysiologyBulgarian Academy of SciencesSofiaBulgaria
  2. 2.Institute of Plant ScienceUniversity of BernBernSwitzerland