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AXY8 encodes an alpha-fucosidase, underscoring the importance of apoplastic metabolism on the fine structure of Arabidopsis cell wall polysaccharides

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons97315

Neumetzler,  L.
Plant Cell Walls - Persson, Max Planck Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Gunl-2011-AXY8 encodes an alph.pdf
(beliebiger Volltext), 641KB

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Zitation

Gunl, M., Neumetzler, L., Kraemer, F., de Souza, A., Schultink, A., Pena, M., et al. (2011). AXY8 encodes an alpha-fucosidase, underscoring the importance of apoplastic metabolism on the fine structure of Arabidopsis cell wall polysaccharides. The Plant Cell, 23(11), 4025-4040. doi:10.1105/tpc.111.089193.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-21E0-D
Zusammenfassung
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.