Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast.
We have expressed a bovine synthetic acyl-CoA-binding protein (ACBP) gene in yeast (Saccharomyces cerevisiae) under the control of the GAL1 promoter. The heterologously expressed bovine ACBP constituted up to 6.4% of total cellular protein and the processing was identical with that of native bovine ACBP, i.e. the initiating methionine was removed and the following serine residue was N-acetylated. The expression of this protein did not affect the growth rate of the cells. Determination of the yeast acyl-CoA pool size showed a close positive correlation between the ACBP content of the cells and the size of the acyl-CoA pool. Thus ACBP can act as an intracellular acyl-CoA pool former. Possible physiological functions of ACBP in cells are discussed.
Mandrup
S
S
Institute of Biochemistry, Odense University, Denmark.
Jepsen
R
R
Skøtt
H
H
Rosendal
J
J
Højrup
P
P
Kristiansen
K
K
Knudsen
J
J
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002417:Cattle; D003001:Cloning, Molecular; D004926:Escherichia coli; D050556:Fatty Acid-Binding Proteins; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D009841:Oligonucleotides; D010957:Plasmids; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae
D000214:Acyl Coenzyme A; D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009841:Oligonucleotides; D011994:Recombinant Proteins