Abstract
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.
Original language | English |
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Journal | FEBS Letters |
Volume | 583 |
Issue number | 7 |
Pages (from-to) | 1159-1163 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 2009 |
Keywords
- Carbohydrate-binding module 20
- Starch-binding domain
- Surface plasmon resonance
- Glucan, water dikinase
- Bioimaging