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Plant Physiol, October 1999, Vol. 121, pp. 665-674

Snow-Mold-Induced Apoplastic Proteins in Winter Rye Leaves Lack Antifreeze Activity1

Mervi Hiilovaara-Teijo,2* Asko Hannukkala, Marilyn Griffith, Xiao-Ming Yu, and Kaarina Pihakaski-Maunsbach3

Department of Biology, Laboratory of Plant Physiology and Molecular Biology, FIN-20014 University of Turku, Turku, Finland (M.H.-T., K.P.-M.); Agricultural Research Centre, Institute of Plant Protection, FIN-31600 Jokioinen, Finland (A.H.); and Department of Biology, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1 (M.G., X.-M.Y.)

During cold acclimation, winter rye (Secale cereale L.) plants secrete antifreeze proteins that are similar to pathogenesis-related (PR) proteins. In this experiment, the secretion of PR proteins was induced at warm temperatures by infection with pink snow mold (Microdochium nivale), a pathogen of overwintering cereals. A comparison of cold-induced and pathogen-induced proteins showed that PR proteins accumulated in the leaf apoplast to a greater level in response to cold. The PR proteins induced by cold and by snow mold were similar when separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and examined by immunoblotting. Both groups of PR proteins contained glucanase-like, chitinase-like, and thaumatin-like proteins, and both groups exhibited similar levels of glucanase and chitinase activities. However, only the PR proteins induced by cold exhibited antifreeze activity. Our findings suggest that the cold-induced PR proteins may be isoforms that function as antifreeze proteins to modify the growth of ice during freezing while also providing resistance to the growth of low-temperature pathogens in advance of infection. Both functions of the cold-induced PR proteins may improve the survival of overwintering cereals.


1 This work was supported by research grants from the Academy of Finland (project no. 29502 to K.P.-M.) and from the Natural Science and Engineering Research Council of Canada (to M.G.).

2 Present address: Dr. Mervi Hiilovaara-Teijo (former name Antikainen), Department of Biosciences, Division of Genetics, P.O. Box 56, FIN-00014 University of Helsinki, Finland.

3 Present address: Department of Cell Biology, Institute of Anatomy, University of Aarhus, DK-8000 Aarhus C, Denmark.

* Corresponding author; e-mail  Mervi.Hiilovaara-Teijo{at}Helsinki.Fi; fax 358-9-708-59079.

© 1999 American Society of Plant Physiologists



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