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J Biol Chem, Vol. 274, Issue 14, 9216-9223, April 2, 1999
,
From the Departments of A computer-based screen of the
Saccharomyces cerevisiae genome identified
YJR019C as a candidate oleate-induced gene.
YJR019C mRNA levels were increased significantly during
growth on fatty acids, suggesting that it may play a role in fatty acid
metabolism. The YJR019C product is highly similar to tesB,
a bacterial acyl-CoA thioesterase, and carries a tripeptide sequence,
alanine-lysine-phenylalanineCOOH, that closely resembles
the consensus sequence for type-1 peroxisomal targeting signals.
YJR019C directed green fluorescence protein to peroxisomes, and
biochemical studies revealed that YJR019C is an abundant component of
purified yeast peroxisomes. Disruption of the YJR019C gene
caused a significant decrease in total cellular thioesterase activity,
and recombinant YJR019C was found to exhibit intrinsic acyl-CoA
thioesterase activity of 6 units/mg. YJR019C also shared significant
sequence similarity with hTE, a human thioesterase that was previously
identified because of its interaction with human immunodeficiency
virus-Nef in the yeast two-hybrid assay. We report here that hTE is
also a peroxisomal protein, demonstrating that thioesterase activity is
a conserved feature of peroxisomes. We propose that YJR019C
and hTE be renamed as yeast and human PTE1 to
reflect the fact that they encode peroxisomal thioesterases. The
physical segregation of yeast and human PTE1 from the cytosolic fatty
acid synthase suggests that these enzymes are unlikely to play a role
in formation of fatty acids. Instead, the observation that PTE1
contributes to growth on fatty acids implicates this thioesterase in
fatty acid oxidation.
Biological Chemistry and
¶ Pediatrics, The Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205 and the § Department of
Physiological Chemistry, Ruhr-Universitat Bochum,
44780 Bochum, Germany
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