TY - JOUR
T1 - Oleate β-oxidation in yeast involves thioesterase but not Yor180c protein that is not a dienoyl-CoA isomerase
AU - Ntamack, André G.
AU - Karpichev, Igor V.
AU - Gould, Stephen J.
AU - Small, Gillian M.
AU - Schulz, Horst
N1 - Funding Information:
This work was supported by U.S. Public Health Service Grant GM008168 from the National Institute of General Medical Sciences and by U.S. Public Health Service Grant RR03060 to Research Centers of Minority Institutions.
PY - 2009/5
Y1 - 2009/5
N2 - The β-oxidation of oleic acid in Saccharomyces cerevisiae (S. cerevisiae) was studied by comparing the growth of wild-type cells on oleic acid or palmitic acid with the growth of mutants that either had a deletion in the YOR180c (DCI1) gene reported to encode Δ3,5,Δ2,4-dienoyl-CoA isomerase (dienoyl-CoA isomerase) or in the PTE1 gene encoding peroxisomal thioesterase 1. Growth of wild-type cells was indistinguishable from that of YOR180c mutant cells on either palmitic acid or oleic acid, whereas the PTE1 mutant grew slower and to a lower density on oleic acid but not on palmitic acid. The identification of 3,5-tetradecadienoic acid in the medium of wild-type cells but not in the medium of the PTE1 mutant proves the operation of the thioesterase-dependent pathway of oleate β-oxidation in S. cerevisiae. Dienoyl-CoA isomerase activity was very low in wild-type cells, fourfold higher in the YOR180c mutant, and not associated with purified Yor180c protein. These observations support the conclusion that the YOR180c gene does not encode dienoyl-CoA isomerase.
AB - The β-oxidation of oleic acid in Saccharomyces cerevisiae (S. cerevisiae) was studied by comparing the growth of wild-type cells on oleic acid or palmitic acid with the growth of mutants that either had a deletion in the YOR180c (DCI1) gene reported to encode Δ3,5,Δ2,4-dienoyl-CoA isomerase (dienoyl-CoA isomerase) or in the PTE1 gene encoding peroxisomal thioesterase 1. Growth of wild-type cells was indistinguishable from that of YOR180c mutant cells on either palmitic acid or oleic acid, whereas the PTE1 mutant grew slower and to a lower density on oleic acid but not on palmitic acid. The identification of 3,5-tetradecadienoic acid in the medium of wild-type cells but not in the medium of the PTE1 mutant proves the operation of the thioesterase-dependent pathway of oleate β-oxidation in S. cerevisiae. Dienoyl-CoA isomerase activity was very low in wild-type cells, fourfold higher in the YOR180c mutant, and not associated with purified Yor180c protein. These observations support the conclusion that the YOR180c gene does not encode dienoyl-CoA isomerase.
KW - Oleic acid
KW - Peroxisomal β-oxidation
KW - Saccharomyces cerevisiae
KW - Thioesterase-dependent pathway
KW - Yor180c protein
KW - Δ,Δ-dienoyl-CoA isomerase
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U2 - 10.1016/j.bbalip.2009.01.026
DO - 10.1016/j.bbalip.2009.01.026
M3 - Article
C2 - 19830908
AN - SCOPUS:64749083953
SN - 1388-1981
VL - 1791
SP - 371
EP - 378
JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
IS - 5
ER -