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Plant Physiol, July 2001, Vol. 126, pp. 1162-1173

Binding Site for Chitin Oligosaccharides in the Soybean Plasma Membrane1

R. Bradley Day,2 Mitsuo Okada, Yuki Ito, Koji Tsukada, Habib Zaghouani, Naoto Shibuya, and Gary Stacey*

Department of Microbiology (R.B.D., H.Z., G.S.) and the Center for Legume Research (R.B.D., G.S.), University of Tennessee, M409 Walters Life Science Building, Knoxville, Tennessee 37996-0845; and the Department of Glycobiology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305, Japan (M.O., Y.I., K.T., N.S.)

Affinity cross-linking of the plasma membrane fraction to an 125I-labeled chitin oligosaccharide led to the identification and characterization of an 85-kD, chitin binding protein in plasma membrane-enriched fractions from both suspension-cultured soybean cells and root tissue. Inhibition analysis indicated a binding preference for larger (i.e. degrees of polymerization = 8) N-acetylated chitin molecules with a 50% inhibition of initial activity value of approximately 50 nM. N-Acetyl-glucosamine and chitobiose showed no inhibitory effects at concentrations as high as 250 µM. It is noteworthy that the major lipo-chitin oligosaccharide Nod signal produced by Bradyrhizobium japonicum was also shown to be a competitive inhibitor of ligand binding. However, the binding site appeared to recognize the chitin portion of the Nod signal, and it is unlikely that this binding activity represents a specific Nod signal receptor. Chitooligosaccharide specificity for induction of medium alkalinization and the generation of reactive oxygen in suspension-cultured cells paralleled the binding activity. Taken together, the presence of the chitin binding protein in the plasma membrane fraction and the specificity and induction of a biological response upon ligand binding suggest a role for the protein as an initial response mechanism for chitin perception in soybean (Glycine max).

1 This work was supported by the Department of Energy (grant no. DE-FG02-97ER-20260 to G.S.) and by a research grant from Bio-oriented Technology Research Advancement Institute (PRO-BRAIN to N.S.).

2 Present address: National Institute of Agrobiological Resources, Department of Biotechnology, Laboratory of Glycobiology, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.

* Corresponding author; e-mail gstacey{at}utk.edu; fax 865- 974-4007.

© 2001 American Society of Plant Physiologists


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