title: Formation of the ether lipids archaetidylglycerol and archaetidylethanolamine in Escherichia coli.
abstract: In archaea, the membrane phospholipids consist of isoprenoid hydrocarbon chains that are ether-linked to a sn-glycerol1-phosphate backbone. This unique structure is believed to be vital for the adaptation of these micro-organisms to extreme environments, but it also reflects an evolutionary marker that distinguishes archaea from bacteria and eukaryotes. CDP-archaeol is the central precursor for polar head group attachment. We examined various bacterial enzymes involved in the attachment of L-serine and glycerol as polar head groups for their promiscuity in recognizing CDP-archaeol as a substrate. Using a combination of mutated bacterial and archaeal enzymes, archaetidylethanolamine (AE) and archaetidylglycerol (AG) could be produced in vitro using nine purified enzymes while starting from simple building blocks. The ether lipid pathway constituted by a set of archaeal and bacterial enzymes was introduced into Escherichia coli, which resulted in the biosynthesis of AE and AG. This is a further step in the reprogramming of E. coli for ether lipid biosynthesis.
authors.affiliation: Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands; The Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands.
authors.forename: Antonella
authors.initials: A
authors.lastname: Caforio
authors.affiliation: Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands; The Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands.
authors.forename: Samta
authors.initials: S
authors.lastname: Jain
authors.affiliation: Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
authors.forename: Peter
authors.initials: P
authors.lastname: Fodran
authors.affiliation: Department of Microbiology, Wageningen University, Dreijenplein 10, 6703HB Wageningen, The Netherlands.
authors.forename: Melvin
authors.initials: M
authors.lastname: Siliakus
authors.affiliation: Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
authors.forename: Adriaan J
authors.initials: AJ
authors.lastname: Minnaard
authors.affiliation: Department of Microbiology, Wageningen University, Dreijenplein 10, 6703HB Wageningen, The Netherlands.
authors.forename: John
authors.initials: J
authors.lastname: van der Oost
authors.affiliation: Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands; The Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands a.j.m.driessen@rug.nl.
authors.forename: Arnold J M
authors.initials: AJ
authors.lastname: Driessen
mesh_terms: D001105:Archaea / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D053898:Biosynthetic Pathways; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D004987:Ethers / Q000737:chemistry / Q000378:metabolism*; D005995:Glyceryl Ethers / Q000737:chemistry / Q000378:metabolism; D008055:Lipids / Q000096:biosynthesis* / Q000737:chemistry; D060847:Metabolic Engineering
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D004987:Ethers; D005995:Glyceryl Ethers; D008055:Lipids; C094417:archaeol lipid
keywords: archaea; ether lipid biosynthesis; liquid chromatography–mass spectrometry (LC–MS); membrane proteins