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Several Thaumatin-Like Proteins Bind to beta -1,3-Glucans1

Jean Trudel, Jean Grenier, Claude Potvin, and Alain Asselin*

Département de Phytologie, Faculté des Sciences de l'Agriculture et de l'Alimentation, Université Laval, Québec, Canada G1K 7P4

Pathogenesis-related proteins from intercellular fluid washings of stressed barley (Hordeum vulgare L.) leaves were analyzed to determine their binding to various water-insoluble polysaccharides. Three proteins (19, 16, and 15 kD) bound specifically to several water-insoluble beta -1,3-glucans. Binding of the barley proteins to pachyman occurred quickly at 22°C at pH 5.0, even in the presence of 0.5 M NaCl, 0.2 M urea, and 1% (v/v) Triton X-100. Bound barley proteins were released by acidic treatments or by boiling in sodium dodecyl sulfate. Acid-released barley proteins could bind again specifically and singly to pachyman. Water-soluble laminarin and carboxymethyl-pachyman competed for the binding of the barley proteins to pachyman. The N-terminal sequence of the 19-kD barley beta -1,3-glucan-binding protein showed near identity to the barley seed protein BP-R and high homology to other thaumatin-like (TL) permatins. The 16-kD barley protein was also homologous to TL proteins, whereas the 15-kD barley protein N-terminal sequence was identical to the pathogenesis-related Hv-1 TL protein. Antifungal barley protein BP-R and corn (Zea mays) zeamatin were isolated by binding to pachyman. Two extracellular proteins from stressed pea (Pisum sativum L.) also bound to pachyman and were homologous to TL proteins.

1   This work was supported by a grant from the Natural Sciences and Engineering Council of Canada and the Conseil des Recherches en Pêche et Agro-Alimentaire du Québec to A.A.
*   Corresponding author; e-mail alain.asselin{at}fsaa.ulaval.ca; fax 1-418-656-7856.

Plant Physiol. (1998) 118: 1431-1438
Copyright Clearance Center:   0032-0889/98/118//08
© 1998 American Society of Plant Physiologists




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