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Sphingolipid C4 hydroxylation influences properties of yeast detergent‐insoluble glycolipid‐enriched membranes
Author(s) -
Idkowiak-Baldys Jolanta,
Grilley Michelle M,
Takemoto Jon Y
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.074
Subject(s) - glycolipid , membrane , yeast , sphingolipid , hydroxylation , chemistry , biochemistry , saccharomyces cerevisiae , chromatography , enzyme
Sphingoid base C4 hydroxylation is required for syringomycin E action on the yeast plasma membrane. Detergent‐insoluble glycolipid‐enriched membranes (DIGs) from a yeast strain lacking C4 hydroxylated sphingoid bases ( sur2 Δ ) are composed of linear membrane fragments instead of vesicular structures observed for wild‐type DIGs, though they have similar lipid compositions and amounts of DIG marker proteins. Light‐scattering bands collected from sur2 Δ after centrifugation of Triton X‐100‐treated cell lysates in continuous density gradients have lower buoyant densities than that of the wild‐type. The results show that C4 hydroxylation influences the physical and structural properties of DIGs and suggest that syringomycin E interacts with lipid rafts.