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Antifreeze Proteins in Winter Rye Leaves Form Oligomeric Complexes1

Xiao-Ming Yu and Marilyn Griffith*

Department of Biology, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1

Antifreeze proteins (AFPs) similar to three pathogenesis-related proteins, a glucanase-like protein (GLP), a chitinase-like protein (CLP), and a thaumatin-like protein (TLP), accumulate during cold acclimation in winter rye (Secale cereale) leaves, where they are thought to modify the growth of intercellular ice during freezing. The objective of this study was to characterize the rye AFPs in their native forms, and our results show that these proteins form oligomeric complexes in vivo. Nine proteins were separated by native-polyacrylamide gel electrophoresis from apoplastic extracts of cold-acclimated winter rye leaves. Seven of these proteins exhibited multiple polypeptides when denatured and separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After isolation of the individual proteins, six were shown by immunoblotting to contain various combinations of GLP, CLP, and TLP in addition to other unidentified proteins. Antisera produced against individual cold-induced winter rye GLP, CLP, and TLP all dramatically inhibited glucanase activity in apoplastic extracts from cold-acclimated winter rye leaves, and each antiserum precipitated all three proteins. These results indicate that each of the polypeptides may be exposed on the surface of the protein complexes. By forming oligomeric complexes, AFPs may form larger surfaces to interact with ice, or they may simply increase the mass of the protein bound to ice. In either case, the complexes of AFPs may inhibit ice growth and recrystallization more effectively than the individual polypeptides.

1   This work was supported by a research grant from the Natural Sciences and Engineering Research Council of Canada to M.G.
*   Corresponding author; e-mail griffith{at}uwaterloo.ca; fax 1-519-746-0614.

Plant Physiol. (1999) 119: 1361-1370
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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