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PLANT PHYSIOLOGY , Vol 109, Issue 3 879-889, Copyright © 1995 by American Society of Plant Biologists
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WHOLE PLANT, ENVIRONMENTAL, AND STRESS PHYSIOLOGY |
Antifreeze Proteins in Winter Rye Are Similar to Pathogenesis-Related Proteins
W. C. Hon, M. Griffith, A. Mlynarz, Y. C. Kwok and DSC. Yang
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada L8N 3Z5 (W.-C.H., D.S.C.Y.)
The ability to control extracellular ice formation during freezing is
critical to the survival of freezing-tolerant plants. Antifreeze proteins,
which are proteins that have the ability to retard ice crystal growth, were
recently identified as the most abundant apoplastic proteins in
cold-acclimated winter rye (Secale cereale L.) leaves. In the experiments
reported here, amino-terminal sequence comparisons, immuno-cross-reactions,
and enzyme activity assays all indicated that these antifreeze proteins are
similar to members of three classes of pathogenesis-related proteins,
namely, endochitinases, endo-[beta]-1,3-glucanases, and thaumatin-like
proteins. Apoplastic endochitinases and endo-[beta]-1,3-glucanases that
were induced by pathogens in freezing-sensitive tobacco did not exhibit
antifreeze activity. Our findings suggest that subtle structural
differences may have evolved in the pathogenesis-related proteins that
accumulate at cold temperatures in winter rye to confer upon these proteins
the ability to bind to ice.
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