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(Received for publication, December 3, 1996, and in revised form, February 4, 1997)
From the cDNA encoding the 280-kDa
acetyl-CoA carboxylase 2 (ACC2) isoform was isolated from human liver
using the polymerase chain reaction. Sequencing the cDNA revealed
an open reading frame of 7,449 base pairs (bp) that encode 2,483 amino
acids (Mr 279,380). Using 5-kilobase pair
cDNA clones as probes, we localized the gene encoding the 280-kDa
human carboxylase to chromosome 12q23. When the cDNA of ACC2 was
compared with that of ACC1, the nucleotide sequences and the predicted
amino acid sequences had about 60 and 80% identity, respectively.
Ser77 and Ser79, which were found to be
critical for the phosphorylation and subsequent inactivation of rat
ACC1 (Ser78 and Ser80 of human ACC1), are
conserved in ACC2 and are represented as Ser219 and
Ser221, respectively. On the other hand,
Ser1200, which is also a phosphorylation site in rat ACC1
(Ser1201 of human ACC1), is not conserved in ACC2. The
homology between the amino acid sequences of the two human
carboxylases, however, is primarily found downstream of residues
Ser78 and Ser81 in human ACC1 and their
equivalents, that is Ser219 and Ser221 in ACC2,
suggesting that the sequence of the first 218 amino acids at the N
terminus of ACC2 represents a unique peptide that accounts, in part,
for the variance between the two carboxylases. Using a cDNA probe
(400 bp) that encodes the N-terminal amino acid residues of ACC2 in
Northern blot analyses of different human and mouse tissues showed that
ACC2 is predominantly expressed in liver, heart, and the skeletal
muscles. Polyclonal antibodies raised against the N-terminal peptide
(amino acid residues 1-220) reacted specifically and equally with
human and rat ACC2 carboxylases, confirming the uniqueness of this
N-terminal peptide and its conservation in animal ACC2. In addition, we
present evidence for the presence of an isoform of ACC2
(Mr 270,000) in human liver that differs from
the 280-kDa ACC2 by the absence of 303 nucleotides that encode 101 amino acids in the region between Arg1114 and
Asp1215. The regulation and physiological significance of
the two ACC2 isoforms remain to be determined.
Volume 272, Number 16,
Issue of April 18, 1997
pp. 10669-10677
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
MOLECULAR CLONING, CHARACTERIZATION, CHROMOSOMAL MAPPING,
AND EVIDENCE FOR TWO ISOFORMS
,
,
Verna and Marrs McLean Department of
Biochemistry and the ¶ Department of Molecular and Human Genetics,
Baylor College of Medicine, Houston, Texas 77030
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