Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast
Research output: Contribution to journal › Journal article › Research › peer-review
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.
|Volume||290 ( Pt 2)|
|Number of pages||5|
|Publication status||Published - 1993|
Keywords: Acyl Coenzyme A; Animals; Base Sequence; Carrier Proteins; Cattle; Cloning, Molecular; Escherichia coli; Fatty Acid-Binding Proteins; Molecular Sequence Data; Neoplasm Proteins; Oligonucleotides; Plasmids; Promoter Regions, Genetic; Recombinant Proteins; Saccharomyces cerevisiae