Content of cardiolipin of the membrane and sensitivity to cationic surfactants in Pseudomonas putida

J Appl Microbiol. 2016 Oct;121(4):1004-14. doi: 10.1111/jam.13238.

Abstract

Aims: To establish the role of cardiolipin (CL) of the membrane in response to the presence of tetradecyltrimethylammonium in Pseudomonas putida A (ATCC 12633).

Methods and results: Two ORFs of Ps. putida A (ATCC 12633), which in Ps. putida KT2440 encode the putative CL synthase genes cls and cls2, were cloned, sequenced and mutated. Only the double mutant lacking cls and cls2 showed a reduction of the CL content, 83% lower than the amount produced by the wild-type. Accompanying this change was a 40% decrease in the content of unsaturated fatty acid. Consequently, the membrane of the mutant was more rigid than the one of the parental strain, as observed using fluorescence polarization techniques. The mutant strain showed reduced viability in the presence of tetradecyltrimethylammonium. The incorporation of exogenous CL into its membrane relieved sensitivity to the cationic detergent.

Conclusions: Pseudomonas Putida cells with low levels of CL die in the presence of tetradecyltrimethylammonium, because they cannot counter the fluidizing effect of the cationic surfactant.

Significance and impact of the study: The modification in the membrane phospholipids composition allows knowing the adaptation strategy of Ps. putida when these bacteria are exposed to cationic surfactant.

Keywords: Pseudomonas putida; adaptation; cardiolipin; cardiolipin synthase genes; cationic surfactants.

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Cardiolipins / analysis
  • Cardiolipins / metabolism
  • Cloning, Molecular
  • Fluorescence Polarization
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Open Reading Frames
  • Phospholipids / metabolism
  • Pseudomonas putida / chemistry
  • Pseudomonas putida / drug effects*
  • Pseudomonas putida / genetics
  • Pseudomonas putida / metabolism
  • Surface-Active Agents / pharmacology*
  • Transferases (Other Substituted Phosphate Groups) / genetics
  • Trimethyl Ammonium Compounds / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Cardiolipins
  • Membrane Proteins
  • Phospholipids
  • Surface-Active Agents
  • Trimethyl Ammonium Compounds
  • Transferases (Other Substituted Phosphate Groups)
  • cardiolipin synthetase
  • tetradecyltrimethylammonium

Associated data

  • GENBANK/KF835427
  • GENBANK/KF835428