Journal
FEBS LETTERS
Volume 583, Issue 7, Pages 1159-1163Publisher
WILEY
DOI: 10.1016/j.febslet.2009.02.045
Keywords
Bioimaging; Carbohydrate-binding module 20; Glucan, water dikinase; Starch-binding domain; Surface plasmon resonance
Funding
- Danish Natural Science Research Council
- Danish Research Council for Technology and Production Sciences
- Carlsberg Foundation
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The family 20 carbohydrate-binding module (CBM20) of the Arabidopsis starch phosphorylator glucan, water dikinase 3 (GWD3) was heterologously produced and its properties were compared to the CBM20 from a fungal glucoamylase (GA). The GWD3 CBM20 has 50-fold lower affinity for cyclodextrins than that from GA. Homology modelling identified possible structural elements responsible for this weak binding of the intracellular CBM20. Differential binding of fluorescein-labelled GWD3 and GA modules to starch granules in vitro was demonstrated by confocal laser scanning microscopy and yellow fluorescent protein-tagged GWD3 CBM20 expressed in tobacco confirmed binding to starch granules in planta. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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