Cardiolipin plays an essential role in the formation of intracellular membranes in Escherichia coli

Biochim Biophys Acta Biomembr. 2017 Jun;1859(6):1124-1132. doi: 10.1016/j.bbamem.2017.03.006. Epub 2017 Mar 9.

Abstract

Mitochondria, chloroplasts and photosynthetic bacteria are characterized by the presence of complex and intricate membrane systems. In contrast, non-photosynthetic bacteria lack membrane structures within their cytoplasm. However, large scale over-production of some membrane proteins, such as the fumarate reductase, the mannitol permease MtlA, the glycerol acyl transferase PlsB, the chemotaxis receptor Tsr or the ATP synthase subunit b, can induce the proliferation of intra cellular membranes (ICMs) in the cytoplasm of Escherichia coli. These ICMs are particularly rich in cardiolipin (CL). Here, we have studied the effect of CL in the generation of these membranous structures. We have deleted the three genes (clsA, clsB and clsC) responsible of CL biosynthesis in E. coli and analysed the effect of these mutations by fluorescent and electron microscopy and by lipid mass spectrometry. We have found that CL is essential in the formation of non-lamellar structures in the cytoplasm of E. coli cells. These results could help to understand the structuration of membranes in E. coli and other membrane organelles, such as mitochondria and ER.

Keywords: Bacteria; Cardiolipin; Electron microscopy; F1Fo-ATPase; Flow cytometry; Fluorescence; Membrane biogenesis; Phospholipid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Proton-Translocating ATPases / genetics
  • Bacterial Proton-Translocating ATPases / metabolism
  • Cardiolipins / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / ultrastructure
  • Escherichia coli / metabolism*
  • Escherichia coli / ultrastructure
  • Fluorescent Dyes / chemistry
  • Gene Deletion
  • Gene Expression
  • Isoenzymes / deficiency
  • Isoenzymes / genetics
  • Membrane Proteins / deficiency*
  • Membrane Proteins / genetics
  • Mitochondria / metabolism*
  • Mitochondria / ultrastructure
  • Time-Lapse Imaging
  • Transferases (Other Substituted Phosphate Groups) / deficiency*
  • Transferases (Other Substituted Phosphate Groups) / genetics

Substances

  • Bacterial Proteins
  • Cardiolipins
  • Fluorescent Dyes
  • Isoenzymes
  • Membrane Proteins
  • Transferases (Other Substituted Phosphate Groups)
  • cardiolipin synthetase
  • Bacterial Proton-Translocating ATPases