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The Cellulase KORRIGAN Is Part of the Cellulose Synthase Complex
Thomas Vain1, Elizabeth Faris Crowell1, Hélène Timpano1
1Institut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, F-78000 Versailles, France (T.V., E.F.C., H.T., E.B., T.D., S.P., S.R., H.H., M.G., S.V.);AgroParisTech, Institut Jean-Pierre Bourgin, F-78000 Versailles, France (T.V., E.F.C., H.T., E.B., T.D., H.H., M.G., S.V.); andWageningen University and Research Plant Breeding, Wageningen University and Research Centre, 6708 PD Wageningen, The Netherlands (N.M., L.M.T.).
Abstract:
Plant growth and organ formation depend on the oriented deposition of load-bearing cellulose microfibrils in the cell wall. Cellulose is synthesized by a large relative molecular weight cellulose synthase complex (CSC), which comprises at least three distinct cellulose synthases. Cellulose synthesis in plants or bacteria also requires the activity of an endo-1,4-β-d-glucanase, the exact function of which in the synthesis process is not known. Here, we show, to our knowledge for the first time, that a leaky mutation in the Arabidopsis (Arabidopsis thaliana) membrane-bound endo-1,4-β-d-glucanase KORRIGAN1 (KOR1) not only caused reduced CSC movement in the plasma membrane but also a reduced cellulose synthesis inhibitor-induced accumulation of CSCs in intracellular compartments. This suggests a role for KOR1 both in the synthesis of cellulose microfibrils and in the intracellular trafficking of CSCs. Next, we used a multidisciplinary approach, including live cell imaging, gel filtration chromatography analysis, split ubiquitin assays in yeast (Saccharomyces cerevisiae NMY51), and bimolecular fluorescence complementation, to show that, in contrast to previous observations, KOR1 is an integral part of the primary cell wall CSC in the plasma membrane.
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