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
Standard
Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast. / Mandrup, S; Jepsen, R; Skøtt, H; Rosendal, J; Højrup, P; Kristiansen, K; Knudsen, J.
In: Biochemical Journal, Vol. 290 ( Pt 2), 1993, p. 369-74.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast
AU - Mandrup, S
AU - Jepsen, R
AU - Skøtt, H
AU - Rosendal, J
AU - Højrup, P
AU - Kristiansen, K
AU - Knudsen, J
N1 - 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
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 8452523
VL - 290 ( Pt 2)
SP - 369
EP - 374
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
ER -
ID: 11231151