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. 1995 Nov;109(3):879–889. doi: 10.1104/pp.109.3.879

Antifreeze proteins in winter rye are similar to pathogenesis-related proteins.

W C Hon 1, M Griffith 1, A Mlynarz 1, Y C Kwok 1, D S Yang 1
PMCID: PMC161389  PMID: 8552719

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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