Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size
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Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size. / Knudsen, J; Faergeman, N J; Skøtt, H; Hummel, R; Børsting, C; Rose, T M; Andersen, J S; Højrup, P; Roepstorff, P; Kristiansen, K.
In: Biochemical Journal, Vol. 302 ( Pt 2), 1994, p. 479-85.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size
AU - Knudsen, J
AU - Faergeman, N J
AU - Skøtt, H
AU - Hummel, R
AU - Børsting, C
AU - Rose, T M
AU - Andersen, J S
AU - Højrup, P
AU - Roepstorff, P
AU - Kristiansen, K
N1 - Keywords: Acyl Coenzyme A; Amino Acid Sequence; Base Sequence; Blotting, Southern; Calorimetry; Carrier Proteins; Diazepam Binding Inhibitor; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Genes, Fungal; Genome, Fungal; Humans; Isoelectric Point; Mass Spectrometry; Molecular Sequence Data; Recombinant Proteins; Saccharomyces; Saccharomyces cerevisiae; Sequence Alignment
PY - 1994
Y1 - 1994
N2 - Acyl-CoA-binding protein (ACBP) is a 10 kDa protein characterized in vertebrates. We have isolated two ACBP homologues from the yeast Saccharomyces carlsbergensis, named yeast ACBP types 1 and 2. Both proteins contain 86 amino acid residues and are identical except for four conservative substitutions. In comparison with human ACBP, yeast ACBPs exhibit 48% (type 1) and 49% (type 2) conservation of amino acid residues. The amino acid sequence of S. carlsbergensis ACBP type 1 was found to be identical with the one ACBP present in Saccharomyces cerevisiae. A recombinant form of this protein was expressed in Escherichia coli and S. cerevisiae, purified, and its acyl-CoA-binding properties were characterized by isoelectric focusing and microcalorimetric analyses. The yeast ACBP was found to bind acyl-CoA esters with high affinity (Kd 0.55 x 10(-10) M). Overexpression of yeast ACBP in S. cerevisiae resulted in a significant expansion of the intracellular acyl-CoA pool. Finally, Southern-blotting analysis of the two genes encoding ACBP types 1 and 2 in S. carlsbergensis strongly indicated that this species is a hybrid between S. cerevisiae and Saccharomyces monacensis.
AB - Acyl-CoA-binding protein (ACBP) is a 10 kDa protein characterized in vertebrates. We have isolated two ACBP homologues from the yeast Saccharomyces carlsbergensis, named yeast ACBP types 1 and 2. Both proteins contain 86 amino acid residues and are identical except for four conservative substitutions. In comparison with human ACBP, yeast ACBPs exhibit 48% (type 1) and 49% (type 2) conservation of amino acid residues. The amino acid sequence of S. carlsbergensis ACBP type 1 was found to be identical with the one ACBP present in Saccharomyces cerevisiae. A recombinant form of this protein was expressed in Escherichia coli and S. cerevisiae, purified, and its acyl-CoA-binding properties were characterized by isoelectric focusing and microcalorimetric analyses. The yeast ACBP was found to bind acyl-CoA esters with high affinity (Kd 0.55 x 10(-10) M). Overexpression of yeast ACBP in S. cerevisiae resulted in a significant expansion of the intracellular acyl-CoA pool. Finally, Southern-blotting analysis of the two genes encoding ACBP types 1 and 2 in S. carlsbergensis strongly indicated that this species is a hybrid between S. cerevisiae and Saccharomyces monacensis.
M3 - Journal article
C2 - 8093000
VL - 302 ( Pt 2)
SP - 479
EP - 485
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
ER -
ID: 11254411