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dc.contributor.authorEscobedo-Hinojosa, W.
dc.contributor.authorVences-Guzmán, M.
dc.contributor.authorSchubotz, F.
dc.contributor.authorSandoval-Calderón, M.
dc.contributor.authorSummons, Roger
dc.contributor.authorLópez-Lara, I.
dc.contributor.authorGeiger, O.
dc.contributor.authorSohlenkamp, C.
dc.identifier.citationEscobedo-Hinojosa, W. and Vences-Guzmán, M. and Schubotz, F. and Sandoval-Calderón, M. and Summons, R. and López-Lara, I. and Geiger, O. et al. 2015. OlsG (Sinac-1600) Is an ornithine lipid N-Methyltransferase from the planctomycete Singulisphaera acidiphila. Journal of Biological Chemistry. 290 (24): pp. 15102-15111.

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 d-nitrogen of OL. Methylation is dependent on the presence of the detergent Triton X-100 and the methyldonor S-adenosylmethionine.

dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc.
dc.titleOlsG (Sinac-1600) Is an ornithine lipid N-Methyltransferase from the planctomycete Singulisphaera acidiphila
dc.typeJournal Article
dcterms.source.titleJournal of Biological Chemistry
curtin.accessStatusOpen access via publisher

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