Abstract
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.
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Abbreviations
- EC:
-
electrical conductivity
- f.m.:
-
fresh mass
- HS:
-
heat stress
- HSP:
-
heat shock proteins
- HSR:
-
recovery after heat stress
- RA:
-
Rubisco activase
- RBP:
-
Rubisco binding protein
- Rubisco LS:
-
Rubisco large subunit
- Rubisco SS:
-
Rubisco small subunit
- Rubisco:
-
ribulose-1,5-bisphosphate carboxylase/oxygenase
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This work was partially supported by Swiss National Science Foundation (Project 31-55289.98).
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Demirevska-Kepova, K., Holzer, R., Simova-Stoilova, L. et al. Heat stress effects on ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco binding protein and Rubisco activase in wheat leaves. Biol Plant 49, 521–525 (2005). https://doi.org/10.1007/s10535-005-0045-2
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DOI: https://doi.org/10.1007/s10535-005-0045-2