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. 1993 Mar 1;290(Pt 2):369–374. doi: 10.1042/bj2900369

Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast.

S Mandrup 1, R Jepsen 1, H Skøtt 1, J Rosendal 1, P Højrup 1, K Kristiansen 1, J Knudsen 1
PMCID: PMC1132282  PMID: 8452523

Abstract

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.

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Selected References

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