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https://hdl.handle.net/2440/13395
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Type: | Journal article |
Title: | Binding interactions between barley thaumatin-like proteins and (1,3)-β-D-glucans: Kinetics, specificity, structural analysis and biological implications |
Other Titles: | Binding interactions between barley thaumatin-like proteins and (1,3)-beta-D-glucans: Kinetics, specificity, structural analysis and biological implications |
Author: | Osmond, R. Hrmova, M. Fontaine, F. Imberty, A. Fincher, G. |
Citation: | The Federation of European Biochemical Societies (FEBS) Journal, 2001; 268(15):4190-4199 |
Publisher: | Blackwell Publishing Ltd |
Issue Date: | 2001 |
ISSN: | 1742-464X 0014-2956 |
Statement of Responsibility: | Ronald I. W. Osmond, Maria Hrmova, Fabien Fontaine, Anne Imberty and Geoffrey B. Fincher |
Abstract: | The specificity and kinetics of the interaction between the pathogenesis-related group of thaumatin-like proteins (PR5) in higher plants and (1,3)-β-D-glucans have been investigated. Two thaumatin-like proteins with 60% amino-acid sequence identity were purified from extracts of germinated barley grain, and were designated HvPR5b and HvPR5c. Purified HvPR5c interacted with insoluble (1,3)-β-D-glucans, but not with cellulose, pustulan, xylan, chitin or a yeast mannoprotein. Tight binding was observed with unbranched and unsubstituted (1,3)-β-D-glucans, and weaker binding was seen if (1,6)-β-linked branch points or β-glucosyl substituents were present in the substrate. The HvPR5b protein interacted weakly with insoluble (1,3)-β-D-glucans and did not bind to any of the other polysaccharides tested. This indicated that only specific barley PR5 isoforms interact tightly with (1,3)-β-D-glucans. The complete primary structures of HvPR5b and HvPR5c were determined and used to construct molecular models of HvPR5b and HvPR5c, based on known three-dimensional structures of related thaumatin-like proteins. The models were examined for features that may be associated with (1,3)-β-D-glucan binding, and a potential (1,3)-β-D-glucan-binding region was located on the surface of HvPR5c. No obvious structural features that would prevent binding of (1,3)-β-D-glucan to HvPR5b were identified, but several of the amino acids in HvPR5c that are likely to interact with (1,3)-β-D-glucans are not present in HvPR5b. |
Keywords: | Hordeum Glucans Polysaccharides beta-Glucans Plant Proteins DNA, Complementary Sweetening Agents Binding Sites Amino Acid Sequence Protein Structure, Secondary Protein Binding Sequence Homology, Amino Acid Kinetics Adsorption Hydrogen-Ion Concentration Models, Molecular Time Factors Molecular Sequence Data |
DOI: | 10.1046/j.1432-1327.2001.02331.x |
Published version: | http://dx.doi.org/10.1046/j.1432-1327.2001.02331.x |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 7 |
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