Disruption of the gene encoding the acyl-CoA-binding protein (ACB1) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae
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Disruption of the gene encoding the acyl-CoA-binding protein (ACB1) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae. / Schjerling, C K; Hummel, R; Hansen, J K; Borsting, C; Mikkelsen, J M; Kristiansen, K; Knudsen, J.
In: Journal of Biological Chemistry, Vol. 271, No. 37, 1996, p. 22514-21.Research output: Contribution to journal › Journal article › peer-review
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TY - JOUR
T1 - Disruption of the gene encoding the acyl-CoA-binding protein (ACB1) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae
AU - Schjerling, C K
AU - Hummel, R
AU - Hansen, J K
AU - Borsting, C
AU - Mikkelsen, J M
AU - Kristiansen, K
AU - Knudsen, J
N1 - Keywords: Acetic Acid; Acyl Coenzyme A; Acyl-CoA Dehydrogenase, Long-Chain; Blotting, Northern; Carrier Proteins; Diazepam Binding Inhibitor; Ethanol; Fatty Acid Desaturases; Fatty Acid Synthetase Complex; Glucose; Lipid Metabolism; Oleic Acid; Saccharomyces cerevisiae
PY - 1996
Y1 - 1996
N2 - The ACB1 gene encoding the acyl-CoA-binding protein (ACBP) was disrupted in Saccharomyces cerevisiae. The disruption did not affect the growth rate on glucose but reduced the growth rate on ethanol slightly. Although the growth rate of the acb1-disrupted cells was unaffected or only slightly affected, the acb1-disrupted strain was unable to compete with wild type cells when grown in mixed culture. The acyl-CoA level in the disrupted cells was increased from 1.5- to 2.5-fold during exponential growth. The increase in the acyl-CoA level was caused solely by an increase in de novo synthesized stearoyl-CoA. Experiments with purified yeast fatty acid synthetase show that it will synthesize long chain acyl-CoAs in the absence of acyl-CoA-binding protein. The addition of ACBP to the incubation medium resulted in a dramatic decrease in the chain length of the synthesized acyl-CoA esters. Despite the fact that the stearoyl-CoA concentration was increased 7-fold and the Delta9-desaturase mRNA level was increased 3-fold, the synthesis of oleic acid was unchanged in the acb1-disrupted strain. The results strongly indicate that ACBP in yeast is involved in the transport of newly synthesized acyl-CoA esters from the fatty acid synthetase to acyl-CoA-consuming processes.
AB - The ACB1 gene encoding the acyl-CoA-binding protein (ACBP) was disrupted in Saccharomyces cerevisiae. The disruption did not affect the growth rate on glucose but reduced the growth rate on ethanol slightly. Although the growth rate of the acb1-disrupted cells was unaffected or only slightly affected, the acb1-disrupted strain was unable to compete with wild type cells when grown in mixed culture. The acyl-CoA level in the disrupted cells was increased from 1.5- to 2.5-fold during exponential growth. The increase in the acyl-CoA level was caused solely by an increase in de novo synthesized stearoyl-CoA. Experiments with purified yeast fatty acid synthetase show that it will synthesize long chain acyl-CoAs in the absence of acyl-CoA-binding protein. The addition of ACBP to the incubation medium resulted in a dramatic decrease in the chain length of the synthesized acyl-CoA esters. Despite the fact that the stearoyl-CoA concentration was increased 7-fold and the Delta9-desaturase mRNA level was increased 3-fold, the synthesis of oleic acid was unchanged in the acb1-disrupted strain. The results strongly indicate that ACBP in yeast is involved in the transport of newly synthesized acyl-CoA esters from the fatty acid synthetase to acyl-CoA-consuming processes.
M3 - Journal article
C2 - 8798418
VL - 271
SP - 22514
EP - 22521
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 37
ER -
ID: 11253748