OlsG (Sinac_1600) Is an Ornithine Lipid N-Methyltransferase from the Planctomycete Singulisphaera acidiphila

J Biol Chem. 2015 Jun 12;290(24):15102-11. doi: 10.1074/jbc.M115.639575. Epub 2015 Apr 29.

Abstract

Ornithine lipids (OLs) are phosphorus-free membrane lipids widespread in bacteria but absent from archaea and eukaryotes. In addition to the unmodified OLs, a variety of OL derivatives hydroxylated in different structural positions has been reported. Recently, methylated derivatives of OLs were described in several planctomycetes isolated from a peat bog in Northern Russia, although the gene/enzyme responsible for the N-methylation of OL remained obscure. Here we identify and characterize the OL N-methyltransferase OlsG (Sinac_1600) from the planctomycete Singulisphaera acidiphila. When OlsG is co-expressed with the OL synthase OlsF in Escherichia coli, methylated OL derivatives are formed. An in vitro characterization shows that OlsG is responsible for the 3-fold methylation of the terminal δ-nitrogen of OL. Methylation is dependent on the presence of the detergent Triton X-100 and the methyldonor S-adenosylmethionine.

Keywords: lipid methylation; membrane lipid; membrane remodeling; phosphatidylcholine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Chromatography, High Pressure Liquid
  • Cloning, Molecular
  • DNA Primers
  • Escherichia coli / genetics
  • Lipids
  • Mass Spectrometry
  • Membrane Lipids / metabolism
  • Methyltransferases / metabolism*
  • Ornithine / analogs & derivatives*
  • Ornithine / metabolism
  • Phylogeny
  • Planctomycetales / enzymology*

Substances

  • DNA Primers
  • Lipids
  • Membrane Lipids
  • ornithine containing aminolipid
  • Ornithine
  • Methyltransferases