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

被引：39

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

页码：1159 / 1163

页数：5

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