title: Cardiolipin plays an essential role in the formation of intracellular membranes in Escherichia coli.
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.
authors.affiliation: Departamento de Biología Molecular and Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Universidad de Cantabria - CSIC - SODERCAN, Santander, Spain.
authors.forename: Gerardo
authors.initials: G
authors.lastname: Carranza
authors.affiliation: Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, Univ Paris Diderot, Sorbonne Paris Cité, PSL Research University, Paris, France.
authors.forename: Federica
authors.initials: F
authors.lastname: Angius
authors.affiliation: Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, Univ Paris Diderot, Sorbonne Paris Cité, PSL Research University, Paris, France.
authors.forename: Oana
authors.initials: O
authors.lastname: Ilioaia
authors.affiliation: Université Paris-Saclay, Institut Paris Saclay d'Innovation Thérapeutique, INSERM, CNRS, - Plateforme SAMM - CHATENAY-MALABRY, France.
authors.forename: Audrey
authors.initials: A
authors.lastname: Solgadi
authors.affiliation: Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, Univ Paris Diderot, Sorbonne Paris Cité, PSL Research University, Paris, France. Electronic address: miroux@ibpc.fr.
authors.forename: Bruno
authors.initials: B
authors.lastname: Miroux
authors.affiliation: Departamento de Biología Molecular and Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Universidad de Cantabria - CSIC - SODERCAN, Santander, Spain. Electronic address: arechagai@unican.es.
authors.forename: Ignacio
authors.initials: I
authors.lastname: Arechaga
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D025243:Bacterial Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism; D002308:Cardiolipins / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D005456:Fluorescent Dyes / Q000737:chemistry; D017353:Gene Deletion; D015870:Gene Expression; D007527:Isoenzymes / Q000172:deficiency / Q000235:genetics; D008565:Membrane Proteins / Q000172:deficiency* / Q000235:genetics; D008928:Mitochondria / Q000378:metabolism* / Q000648:ultrastructure; D059008:Time-Lapse Imaging; D017855:Transferases (Other Substituted Phosphate Groups) / Q000172:deficiency* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D002308:Cardiolipins; D005456:Fluorescent Dyes; D007527:Isoenzymes; D008565:Membrane Proteins; D017855:Transferases (Other Substituted Phosphate Groups); C100091:cardiolipin synthetase; D025243:Bacterial Proton-Translocating ATPases
keywords: Bacteria; Cardiolipin; Electron microscopy; F1Fo-ATPase; Flow cytometry; Fluorescence; Membrane biogenesis; Phospholipid