부산대학교 도서관

To authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1111/j.1365-313X.2009.03785.x Byline: Cecile Herve (1), Artur Rogowski (2), Harry J. Gilbert (2), J. Paul Knox (1,*) Keywords: plant cell walls; xylan; carbohydrate-binding module; pectate lyase; xylanase; fluorescence quantification Abstract: Summary The capacity of four xylan-directed probes (carbohydrate-binding modules CfCBM2b-1-2 and CjCBM15; monoclonal antibodies LM10 and LM11) to recognize xylan polysaccharides in primary and secondary cell walls of tobacco stem sections has been determined. Enzymatic removal of pectic homogalacturonan revealed differential recognition of xylans in restricted regions of cortical primary cell walls. Monoclonal antibody binding to these exposed xylans was more sensitive to xylanase action than carbohydrate-binding module (CBM) binding. In contrast, the recognition of xylans by CBMs in secondary cell walls of the same organ was more sensitive to xylanase action than the recognition of xylans by the monoclonal antibodies. A methodology was developed to quantify indirect immunofluorescence intensities, and to evaluate xylanase impacts. The four xylan probes were also used to detect xylan populations in chromatographic separations of solubilized cell wall materials from tobacco stems. Altogether, these observations reveal the heterogeneity of the xylans in plant cell walls. They indicate that although CBM and antibody probes can exhibit similar specificities against solubilized polymers, they can have differential capacities for xylan recognition in muro, and that the access of molecular probes and enzymes to xylan epitopes/ligands also varies between primary and secondary cell walls that are present in the same organ. Author Affiliation: (1)Centre for Plant Sciences, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK (2)Institute for Cell and Molecular Biosciences, Newcastle University, The Medical School, Newcastle-upon-Tyne NE2 4HH, UK Article History: Received 12 November 2008; revised 11 December 2008; accepted 17 December 2008; published online 5 February 2009. Article note: (*) For correspondence (fax +44 113 3433144; e-mail j.p.knox@leeds.ac.uk).