AXY8 Encodes an α-Fucosidase, Underscoring the Importance of Apoplastic Metabolism on the Fine Structure of Arabidopsis Cell Wall Polysaccharides

被引：71

作者：

Guenl, Markus ^{[1
]}

Neumetzler, Lutz ^{[2
]}

Kraemer, Florian ^{[1
]}

de Souza, Amancio ^{[1
]}

Schultink, Alex ^{[1
]}

Pena, Maria ^{[3
]}

York, William S. ^{[3
]}

Pauly, Markus ^{[1
]}

机构：

[1] Univ Calif Berkeley, Berkeley, CA 94720 USA

[2] Max Planck Inst Mol Plant Physiol, D-14476 Potsdam, Germany

[3] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA

来源：

PLANT CELL | 2011年 / 23卷 / 11期

基金：

美国国家卫生研究院;

关键词：

XYLOGLUCAN OLIGOSACCHARIDES; GOLGI-APPARATUS; FUCOSYLATED XYLOGLUCAN; GROWTH; GENE; THALIANA; PLANTS; ENDOTRANSGLYCOSYLASE; BIOSYNTHESIS; TRANSFERASE;

D O I：

10.1105/tpc.111.089193

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：

An Arabidopsis thaliana mutant with an altered structure of its hemicellulose xyloglucan (XyG; axy-8) identified by a forward genetic screen facilitating oligosaccharide mass profiling was characterized. axy8 exhibits increased XyG fucosylation and the occurrence of XyG fragments not present in the wild-type plant. AXY8 was identified to encode an alpha-fucosidase acting on XyG that was previously designated FUC95A. Green fluorescent protein fusion localization studies and analysis of nascent XyG in microsomal preparations demonstrated that this glycosylhydrolase acts mainly on XyG in the apoplast. Detailed structural analysis of XyG in axy8 gave unique insights into the role of the fucosidase in XyG metabolism in vivo. The genetic evidence indicates that the activity of glycosylhydrolases in the apoplast plays a major role in generating the heterogeneity of XyG side chains in the wall. Furthermore, without the dominant apoplastic glycosylhydrolases, the XyG structure in the wall is mainly composed of XXXG and XXFG subunits.

引用

页码：4025 / 4040

页数：16

共 81 条

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