A CBM20 low-affinity starch-binding domain from glucan, water dikinase

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...

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Veröffentlicht in:	FEBS letters 2009-04, Vol.583 (7), p.1159-1163
Hauptverfasser:	Christiansen, Camilla, Hachem, Maher Abou, Glaring, Mikkel A., Viksø-Nielsen, Anders, Sigurskjold, Bent W., Svensson, Birte, Blennow, Andreas
Format:	Artikel
Sprache:	eng
Schlagworte:	Arabidopsis Arabidopsis - cytology Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Aspergillus niger - enzymology Aspergillus niger - genetics Bioimaging carbohydrate-binding module Carbohydrate-binding module 20 CBM CLSM confocal laser scanning microscopy Cyclodextrins - chemistry Cytoplasmic Granules - genetics Cytoplasmic Granules - metabolism Fungal Proteins - genetics Fungal Proteins - metabolism Gene Expression Glucan 1,4-alpha-Glucosidase - genetics Glucan 1,4-alpha-Glucosidase - metabolism Glucan, water dikinase glucoamylase GWD Microscopy, Confocal - methods Nicotiana - genetics Phosphotransferases (Paired Acceptors) - genetics Phosphotransferases (Paired Acceptors) - metabolism Protein Binding - physiology Protein Structure, Tertiary - physiology SBD SPR Starch - genetics Starch - metabolism Starch-binding domain Structural Homology, Protein Surface plasmon resonance yellow fluorescent protein YFP
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Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2009.02.045