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J Biol Chem, Vol. 273, Issue 18, 11062-11068, May 1, 1998
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From the The Saccharomyces cerevisiae gene
SYR2, necessary for growth inhibition by the cyclic
lipodepsipeptide syringomycin E, is shown to be required for
4-hydroxylation of long chain bases in sphingolipid biosynthesis. Four
lines of support for this conclusion are presented: (a) the
predicted Syr2p shows sequence similarity to diiron-binding membrane
enzymes involved in oxygen-dependent modifications of
hydrocarbon substrates, (b) yeast strains carrying a
disrupted SYR2 allele produced sphingoid long chain bases
lacking the 4-hydroxyl group present in wild type strains,
(c) 4-hydroxylase activity was increased in microsomes
prepared from a SYR2 overexpression strain, and
(d) the syringomycin E resistance phenotype of a
syr2 mutant strain was suppressed when grown under
conditions in which exogenous 4-hydroxysphingoid long chain bases were
incorporated into sphingolipids. The syr2 strain produced
wild type levels of sphingolipids, substantial levels of hydroxylated
very long chain fatty acids, and the full complement of normal yeast
sphingolipid head groups. These results show that the SYR2
gene is required for the 4-hydroxylation reaction of sphingolipid long
chain bases, that this hydroxylation is not essential for growth, and
that the 4-hydroxyl group of sphingolipids is necessary for
syringomycin E action on yeast.
Department of Biology, Utah State
University, Logan, Utah 84322 and the § Department of
Biochemistry and the Lucille P. Markey Cancer Center, University of
Kentucky, Lexington, Kentucky 40536
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