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Published on: February 4, 2013
Ethylene induces antifreeze activity in winter rye leaves
X M Yu1, M Griffith, S B Wiseman
1Department of Biology, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1.
Ethylene regulates antifreeze activity in winter rye (Secale cereale) leaves, increasing protein accumulation and activity in response to cold and drought. Salicylic acid did not induce this response.
Area of Science:
- Plant Physiology
- Molecular Biology
- Biochemistry
Background:
- Winter rye (Secale cereale) leaves exhibit antifreeze activity induced by cold temperatures.
- This activity is attributed to six antifreeze proteins (AFPs) accumulating in the apoplast during cold acclimation.
- These AFPs are structurally related to pathogenesis-related proteins like glucanases, chitinases, and thaumatin-like proteins.
Purpose of the Study:
- To investigate the role of ethylene and salicylic acid in regulating antifreeze activity in winter rye.
- To understand the signaling pathways involved in AFP accumulation and cold tolerance.
Main Methods:
- Treatment of nonacclimated winter rye plants with ethylene and salicylic acid.
- Induction of antifreeze activity using ethylene-releasing agents (ethephon, 1-aminocyclopropane-1-carboxylate) and inhibition with AgNO(3).
- Analysis of apoplastic protein accumulation via immunoblotting and measurement of antifreeze activity under cold (5°C) and drought stress.
Main Results:
- Ethylene treatment significantly increased antifreeze activity and apoplastic protein concentration in rye leaves.
- Salicylic acid treatment did not induce antifreeze activity.
- Immunoblotting confirmed the presence of glucanases, chitinases, and thaumatin-like proteins among the accumulated proteins.
- Cold and drought stress induced both ethylene production and antifreeze activity in winter rye.
Conclusions:
- Ethylene plays a crucial role in mediating antifreeze activity in winter rye.
- Ethylene signaling is involved in the plant's response to cold and drought stress.
- The findings suggest a link between stress responses and the accumulation of antifreeze proteins.
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