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Requirement of sphingolipid α‐hydroxylation for fungicidal action of syringomycin E
Author(s) -
Hama Hiroko,
Young Debra A.,
Radding Jeffrey A.,
Ma Doreen,
Tang Julia,
Stock Stephen D.,
Takemoto Jon Y.
Publication year - 2000
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/s0014-5793(00)01821-4
Subject(s) - sphingolipid , biochemistry , biology , yeast , saccharomyces cerevisiae , hydroxylation , gene , pseudomonas syringae , fungicide , microbiology and biotechnology , enzyme , botany
Syringomycin E is an antifungal cyclic lipodepsinonapeptide produced by Pseudomonas syringae pv. syringae . To understand the mechanism of action of syringomycin E, a novel resistant Saccharomyces cerevisiae strain, BW7, was isolated and characterized. Lipid analyses revealed that BW7 contained only the hydrophobic subspecies of sphingolipids that are normally minor components in wild type strains. This aberrant sphingolipid composition was the result of lack of α‐hydroxylation of the amide‐linked very long chain fatty acids, suggesting a defective sphingolipid α‐hydroxylase encoded by the FAH1 gene. A yeast strain that lacks the FAH1 gene was resistant to syringomycin E, and failed to complement BW7. These results demonstrate that BW7 carries a mutation in the FAH1 gene, and that the lack of α‐hydroxylated very long chain fatty acids in yeast sphingolipids confers resistance to syringomycin E.