| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2050388 | FEBS Letters | 2009 | 5 Pages |
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.
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Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Camilla Christiansen, Maher Abou Hachem, Mikkel A. Glaring, Anders Viksø-Nielsen, Bent W. Sigurskjold, Birte Svensson, Andreas Blennow,