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

Camilla Christiansen; Maher Abou Hachem; M.A. Glaring; A. Vikso-Nielsen; B.W. Sigurskjold; Birte Svensson; A. Blennow

doi:10.1016/j.febslet.2009.02.045

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

Camilla Christiansen
, Maher Abou Hachem
, M.A. Glaring
, A. Vikso-Nielsen
, B.W. Sigurskjold
, Birte Svensson
, A. Blennow

Research output: Contribution to journal › Journal article › Research › peer-review

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
Journal	FEBS Letters
Volume	583
Issue number	7
Pages (from-to)	1159-1163
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2009.02.045
Publication status	Published - 2009

Keywords

Carbohydrate-binding module 20
Starch-binding domain
Surface plasmon resonance
Glucan, water dikinase
Bioimaging

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10.1016/j.febslet.2009.02.045

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

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.",

keywords = "Carbohydrate-binding module 20, Starch-binding domain, Surface plasmon resonance, Glucan, water dikinase, Bioimaging",

author = "Camilla Christiansen and \{Abou Hachem\}, Maher and M.A. Glaring and A. Vikso-Nielsen and B.W. Sigurskjold and Birte Svensson and A. Blennow",

year = "2009",

doi = "10.1016/j.febslet.2009.02.045",

language = "English",

volume = "583",

pages = "1159--1163",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "7",

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TY - JOUR

T1 - A CBM20 low-affinity starch-binding domain from glucan, water dikinase

AU - Christiansen, Camilla

AU - Abou Hachem, Maher

AU - Glaring, M.A.

AU - Vikso-Nielsen, A.

AU - Sigurskjold, B.W.

AU - Svensson, Birte

AU - Blennow, A.

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

KW - Carbohydrate-binding module 20

KW - Starch-binding domain

KW - Surface plasmon resonance

KW - Glucan, water dikinase

KW - Bioimaging

U2 - 10.1016/j.febslet.2009.02.045

DO - 10.1016/j.febslet.2009.02.045

M3 - Journal article

C2 - 19275898

SN - 0014-5793

VL - 583

SP - 1159

EP - 1163

JO - FEBS Letters

JF - FEBS Letters

IS - 7

ER -

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

Abstract

Keywords

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