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Systematic Identification of Cyclic-di-GMP Binding Proteins in Vibrio cholerae Reveals a Novel Class of Cyclic-di-GMP-Binding ATPases Associated with Type II Secretion Systems

Fig 3

C-di-GMP binds to V. cholerae and P. aeruginosa homologs of MshE.

(A) Average fraction bound 32P-c-di-GMP of E. coli whole cell lysate expressing Vibrio cholerae and Pseudomonas aeruginosa homologs of MshE. The dashed red line indicates background binding for a vector control strain. All data are average of three independent assays and standard deviation is indicated by error bars. (B) Unrooted phylogenetic tree of the T2SSE_N domain. Protein sequences present in the tree corresponding to proteins analyzed for c-di-GMP binding are highlighted in green (binds c-di-GMP), red (does not bind), or blue (candidate binding protein). The dark grey background corresponds to primarily type IV pili PilB sequences, and the light grey background corresponds to type II secretion protein E ATPase sequences. (C, D) Sub-trees containing VC0405 or PA14_29490 and closely related proteins.

Fig 3

doi: https://doi.org/10.1371/journal.ppat.1005232.g003