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

被引：38
|
作者：
Christiansen, Camilla [1 ,2 ]
Abou Hachem, Maher [1 ]
Glaring, Mikkel A. [2 ]
Vikso-Nielsen, Anders [3 ]
Sigurskjold, Bent W. [4 ]
Svensson, Birte [1 ]
Blennow, Andreas [2 ]
机构：
[1] Tech Univ Denmark, Dept Syst Biol, DK-2800 Lyngby, Denmark
[2] Univ Copenhagen, Fac Life Sci, Dept Plant Biol & Biotechnol, VKR Res Ctr, DK-1871 Frederiksberg, Denmark
[3] Novozymes AS, DK-2880 Bagsvaerd, Denmark
[4] Univ Copenhagen, Dept Biol, DK-2100 Copenhagen O, Denmark
来源：
FEBS LETTERS | 2009年 / 583卷 / 07期
关键词：
Bioimaging; Carbohydrate-binding module 20; Glucan; water dikinase; Starch-binding domain; Surface plasmon resonance; ASPERGILLUS-NIGER GLUCOAMYLASE; ALPHA-GLUCAN; RAW-STARCH; ARABIDOPSIS; CYCLODEXTRIN; DEGRADATION; METABOLISM; EXPRESSION; AMYLOSE; GRANULE;
D O I：
10.1016/j.febslet.2009.02.045
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：1159 / 1163
页数：5
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