Figure 2 | Scientific Reports

Figure 2

From: Investigation of the phosphorylation of Bacillus subtilis LTA synthases by the serine/threonine kinase PrkC

Figure 2

PrkC interacts with YfnI. Interactions detected by bacterial two-hybrid assay. Interactions between the catalytic domain of the kinase, PrkCc (WT or mutated for the catalytic residue K40A) and the entire protein YfnI fused to T18 and T25 domains of the adenylate cyclase respectively are presented. Zip was used as a positive control. BTH101 transformed with the empty vectors T18 and T25, the empty vector T25 and vector T18-PrkCc or the empty vector T18 and vector T25-YfnI used as negative controls.

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