Journal article

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Structural characterization of suppressor lipids by high-resolution mass spectrometry

  • Rovillos, Mary Joy Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense, Denmark
  • Pauling, Josch Konstantin Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense, Denmark
  • Hannibal-Bach, Hans Kristian Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense, Denmark
  • Vionnet, Christine Division of Biochemistry, Department of Biology, University of Fribourg, Switzerland
  • Conzelmann, Andreas Division of Biochemistry, Department of Biology, University of Fribourg, Switzerland
  • Ejsing, Christer S. Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense, Denmark
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    30.10.2016
Published in:
  • Rapid Communications in Mass Spectrometry. - 2016, vol. 30, no. 20, p. 2215–2227
English Rationale: Suppressor lipids were originally identified in 1993 and reported to encompass six lipid classes that enable Saccharomyces cerevisiae to live without sphingolipids. Structural characterization, using non-mass spectrometric approaches, revealed that these suppressor lipids are very long chain fatty acid (VLCFA)- containing glycerophospholipids with polar head groups that are typically incorporated into sphingolipids. Here we report, for the first time, the structural characterization of the yeast suppressor lipids using high-resolution mass spectrometry.Methods: Suppressor lipids were isolated by preparative chromatography and subjected to structural characterization using hybrid quadrupole time-of-flight and ion trap-orbitrap mass spectrometry.Results: Our investigation recapitulates the overall structural features of the suppressor lipids and provides an in-depth characterization of their fragmentation pathways. Tandem mass analysis identified the positionally defined molecular lipid species phosphatidylinositol (PI) 26:0/16:1, PI mannoside (PIM) 16:0/26:0 and PIM inositol-phosphate (PIMIP) 16:0/26:0 as abundant suppressor lipids. This finding differs from the original study that only inferred the positional isomer PI 16:0/26:0 and prompts new insight into the biosynthesis of suppressor lipids. Moreover, we also report the identification of a novel suppressor lipid featuring an amino sugar residue linked to a VLCFA-containing PI molecule.Conclusions: Fragmentation pathways of yeast suppressor lipids have been delineated. In addition, the fragmentation information has been added to our open source ALEX lipid database to support automated identification and quantitative monitoring of suppressor lipids in yeast and bacteria that produce similar lipid molecules.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biological sciences
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/305246
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