Fig. 2: Activity readouts of different Cgs constructs.
From: Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens
a In vitro CβG synthesis by Cgs proteoliposomes. MALDI-TOF analysis of reaction products reveals the characteristic size distribution of CβG species. Addition of phosphate in the sample buffer (magenta) results in the synthesis of shorter glucan chains, indicating that the length control depends on the activity of the GP phosphorylase. The number of Glc molecules within the glucan chain and the measured molecular weights are indicated. b Hypoosmotic growth assay showing the role of different domains of Cgs in its function. The Δcgs mutant was complemented by plasmid-encoded cgs variants. Substitutions of key residues of the GT and CY domains abolish Cgs activity. While the catalytic residue of the GP domain is not essential, truncation of the entire CTD (Cgs1-1587) or its part (Cgs1-1846) leads to loss of activity. Error bars represent standard deviation (SD) of three biological replicates (n = 3). Source data are provided as a Source Data file.
