Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 371-378 |
| Number of pages | 8 |
| Journal | Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids |
| Volume | 1791 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2009 |
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Keywords
- Δ,Δ-dienoyl-CoA isomerase
- Oleic acid
- Peroxisomal β-oxidation
- Saccharomyces cerevisiae
- Thioesterase-dependent pathway
- Yor180c protein
ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
Cite this
Oleate β-oxidation in yeast involves thioesterase but not Yor180c protein that is not a dienoyl-CoA isomerase. / Ntamack, André G.; Karpichev, Igor V.; Gould, Stephen J; Small, Gillian M.; Schulz, Horst.
In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, Vol. 1791, No. 5, 05.2009, p. 371-378.Research output: Contribution to journal › Article
}
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
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 - Δ,Δ-dienoyl-CoA isomerase
KW - Oleic acid
KW - Peroxisomal β-oxidation
KW - Saccharomyces cerevisiae
KW - Thioesterase-dependent pathway
KW - Yor180c protein
UR - http://www.scopus.com/inward/record.url?scp=64749083953&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=64749083953&partnerID=8YFLogxK
U2 - 10.1016/j.bbalip.2009.01.026
DO - 10.1016/j.bbalip.2009.01.026
M3 - Article
C2 - 19830908
AN - SCOPUS:64749083953
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
SN - 1388-1981
IS - 5
ER -