Please use this identifier to cite or link to this item: http://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: 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
RMID: 0020010117
DOI: 10.1046/j.1432-1327.2001.02331.x
Appears in Collections:Agriculture, Food and Wine publications

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