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Discovery of a bifunctional acyltransferase responsible for ornithine lipid synthesis in S erratia proteamaculans
Author(s) -
VencesGuzmán Miguel Ángel,
Guan Ziqiang,
EscobedoHinojosa Wendy Itzel,
BermúdezBarrientos José Roberto,
Geiger Otto,
Sohlenkamp Christian
Publication year - 2015
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.12562
Subject(s) - biology , microbiology and biotechnology , bacteria , proteobacteria , biochemistry , 16s ribosomal rna , genetics
Summary Ornithine lipids ( OL s) are phosphorus‐free membrane lipids that can be formed by many bacteria but that are absent from archaea and eukaryotes. A function for OL s in stress conditions and in host–bacteria interactions has been shown in some bacteria. Some bacterial species have been described that can form OL s, but lack the known genes ( ols BA ) involved in its biosynthesis, which implied the existence of a second pathway. Here we describe the bifunctional protein OlsF from S erratia proteamaculans involved in OL formation. Expression of OlsF and its homologue from F lavobacterium johnsoniae in E scherichia coli causes OL formation. Deletion of OlsF in S . proteamaculans caused the absence of OL formation. Homologues of OlsF are widely distributed among γ‐, δ‐ and ε‐ P roteobacteria and in the C ytophaga ‐ F lavobacterium ‐ B acteroidetes group of bacteria, including several well‐studied pathogens for which the presence of OL s has not been suspected, such as for example V ibrio cholerae and K lebsiella pneumonia . Using genomic data, we predict that about 50% of bacterial species can form OL s.