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Figure 3 | BMC Genomics

Figure 3

From: A network-based approach to identify substrate classes of bacterial glycosyltransferases

Figure 3

Consensus networks derived for each of the predicted substrate classes of putative GTs in L. rhamnosus GG. Consensus networks show all GTs, having the same substrate class, together with their protein neighbors that are hypothesized to contribute to the same common glycosylation mechanism as the one the GTs are involved in. On the consensus networks, nodes are proteins than can either be GTs (green nodes), transmembrane proteins (orange nodes) or proteins containing glycosylation signals (violet nodes). Membrane associations established between GTs and transmembrane proteins are represented by blue edges while predicted substrate relations between GT and proteins containing glycosylation signals are represented by yellow edges. Black edges refer to interactions between predicted GTs. If the local network neighborhood of GTs (local subnetwork) belonging to the same substrate class shows enrichment in more than one GO category (e.g. both the GO terms of EPS and glycogen biosynthesis), the consensus network is shown for each of the enriched GO categories. A: consensus networks involving GTs, predicted to glycosylate saccharides. Note that here two independent consensus networks were derived corresponding to respectively extracellular and intracellular PS biosynthesis. B: consensus network involving GTs, predicted to glycosylate peptidoglycan (PG). C: consensus network involving GTs, predicted to glycosylate lipids. D: consensus networks involving GTs, predicted to glycosylate proteins. Three independent consensus networks were derived corresponding to respectively cell cycle regulation, protein translation and DNA metabolic processes. Our analysis suggests substrate promiscuity for MurG, PBP1A, PBP1B and PBPA, all of which were predicted to be involved in the glycosylation of both peptidoglycan and proteins.

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