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Research article

The peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14

  1. Christian Pustelny1,3,†,*,
  2. Stephan Brouwer1,3,†,
  3. Mathias Müsken1,3,
  4. Agata Bielecka1,3,
  5. Andreas Dötsch1,3,
  6. Manfred Nimtz2,
  7. Susanne Häussler1,3

Article first published online: 28 DEC 2012

DOI: 10.1111/1462-2920.12040

Issue

Environmental Microbiology

Environmental Microbiology

Special Issue: Environmental Ecology of Pathogens and Resistances

Volume 15, Issue 2, pages 597–609, February 2013

Additional Information

How to Cite

Pustelny, C., Brouwer, S., Müsken, M., Bielecka, A., Dötsch, A., Nimtz, M. and Häussler, S. (2013), The peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14. Environmental Microbiology, 15: 597–609. doi: 10.1111/1462-2920.12040

Author Information

  1. 1

    Department of Molecular Bacteriology, Helmholtz Center for Infection Research, Braunschweig, Germany

  2. 2

    Cellular Proteome Research Group, Helmholtz Center for Infection Research, Braunschweig, Germany

  3. 3

    Institute of Molecular Bacteriology, Twincore, Center for Clinical and Experimental Infection Research, a joint venture of the Helmholtz Center of Infection Research and the Hannover Medical School, Hannover, Germany

  1. †

    The first two authors made an equal contribution to the work.

*For correspondence. E-mail Christian.pustelny@helmholtz-hzi.de; Tel. (+49) 53161813152; Fax (+49) 53161813099.

  1. †

    The first two authors made an equal contribution to the work.

Publication History

  1. Issue published online: 28 JAN 2013
  2. Article first published online: 28 DEC 2012
  3. Accepted manuscript online: 9 NOV 2012 04:55AM EST
  4. Manuscript Accepted: 2 NOV 2012
  5. Manuscript Received: 10 MAY 2012

Funded by

  • ERC. Grant Number: RESISTOME [260276]
  • Helmholtz International Graduate School for Infection Research. Grant Number: VH-GS-202

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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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