The Arabidopsis COBRA protein facilitates cellulose crystallization at the plasma membrane
Résumé
Mutations in the Arabidopsis COBRA gene lead to defects in cellulose synthesis but the function of COBRA is unknown. Here we present evidence that COBRA localizes to discreet particles in the plasma membrane and is sensitive to inhibitors of cellulose synthesis, suggesting that COBRA and the cellulose synthase complex reside in very close proximity on the plasma membrane. Live-cell imaging of cellulose synthesis indicated that, once initiated, cellulose synthesis appeared to proceed normally in the cobra mutant. Using isothermal calorimetry, COBRA was found to bind individual beta-1,4-linked glucan chains with a KA of 3.2muM. Competition assays suggests that COBRA binds individual beta-1,4-linked glucan chains with higher affinity than crystalline cellulose. Solid-state nuclear magnetic resonance (SSNMR) studies of the cell wall of the cobra mutant also indicated that, in addition to decreases in cellulose amount, the properties of the cellulose fibrils and other cell wall polymers differed from wild type by being less crystalline and having an increased number of reducing ends. We interpret the available evidence as suggesting that COBRA facilitates cellulose crystallization from the emerging beta-1,4 glucan chains by acting as a ''polysaccharide chaperone''.
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