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(Received for publication, June 7, 1996, and in revised form, September 3, 1996)
From the The cDNA encoding rat very long-chain
acyl-CoA synthetase (VLACS) was cloned, using degenerative primers
synthesized according to the partial amino acid sequences of the
peptide fragments of the purified rat liver enzyme. The longest
cDNA insert was 2972 base pairs with a 1860-base pair open reading
frame encoding 620 amino acids. The calculated molecular mass of 70,692 daltons was consistent with size of the purified enzyme. In Northern
blot analysis, a single band was detected at the position of about 3 kilobases, corresponding to the size of the cloned cDNA.
cDNA-directed expression in Escherichia coli resulted
in accumulation of expressed protein, as an inclusion body. An antibody
was raised using this expressed protein to characterize the cDNA
and the enzyme. The subcellular localization of VLACS in peroxisomes
and microsomes was demonstrated in Western blot analysis. The specific
activity and the substrate specificity of the cDNA expressed enzyme
in COS-1 cells were consistent with those of the purified rat enzyme. The predicted amino acid sequence of VLACS had a high sequence similarity to fatty acid transport protein (Schaffer, J. E., and Lodish, H. F. (1994) Cell 79, 427-436), and was considered
to have domains for adenylation and thioester formation. The entire structure of VLACS was dissimilar to that of long-chain acyl-CoA synthetase (Suzuki, H., Kawarabayashi, Y., Kondo, Y., Abe, T., Nishikawa, K., Kimura, S., Hashimoto, T., and Yamamoto, T. (1990) J. Biol. Chem. 265, 8681-8685), except for the
domains.
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30360-30365
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
and
Department of Pediatrics, Gifu University
School of Medicine, Gifu 500, Japan and the ¶ Department of
Biochemistry, Shinshu University School of Medicine, Matsumoto,
Nagano 390, Japan
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