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emi12040-sup-0001-si.tif9745K

Fig. S1. Multiple protein sequence alignment between P. aeruginosa PrmC and various homologues. Protein sequence alignment was created with clustalw2 and visualized with Boxshade 3.31 (Mobyle@Pasteur-v1.0.4). Background colour indicate different residues (white), similar residues (grey) and identical residues (black) in direct comparison with P. aeruginosa PrmC.

emi12040-sup-0002-si.tif3282K

Fig. S2. Autoradiogram of PrmC-dependent methylated PrfA. Cell lysates from PA14_prmC pME6032prfA + purified PrmC (1); PA14_prmC pME6032prfA (2); PA14_prmC pME6032 + purified PrmC (3) and PA14_prmC pME6032 (4) were mixed with 0.6 μM [3H-methyl]-SAM and incubated at 37°C for 30 min. Lane 5 shows the PageRuler Prestained Protein Ladder from Thermo Scientific. On the top panel (A) a NuPAGE 10% Bis-Tris gel was used to separate each reaction. The lower panel (B) shows the corresponding autoradiogram illustrating an intensive methylation reaction of PrfA in the presence of PrmC.

emi12040-sup-0003-si.docx1384K

Table S1. Pyocyanin restoration by pqsE in PA14 transposon mutants that did not respond with an enhanced pyocyanin production after exogenous addition of AQ extracts.

Table S2. List of selected genes affected by PrmC identified by RNA seq.

Table S3. Strains, plasmids and primers used in this work.

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