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J. Biol. Chem., Vol. 265, Issue 13, 7308-7317, May, 1990
SL Weldon, A Rando, AS Matathias, Y Hod, PA Kalonick, S Savon, JS Cook and RW Hanson
The amino acid sequence of the mitochondrial form of phosphoenolpyruvate
carboxykinase (GTP) (EC 4.1.1.32) (PEPCK-M) from the chicken was deduced
from the 3571 nucleotide sequence of three overlapping cDNA clones. The
derived protein sequence, which includes 607 amino acids of the mature
enzyme and a leader sequence, was aligned with nine tryptic peptides of
PEPCK-M and the primary sequence of the cytosolic form of PEPCK from
chicken. Secondary structure predictions for the two PEPCK isozymes
indicated similar packing elements of conserved, hydrophobic beta strands
in the central core of the primary sequence. This core protein, which
contained three GTP-binding consensus elements, was 80% identical in the
two chicken isozymes, although the overall level of identity was only 63%
for amino acids and 60% for nucleotides. The untranslated regions of the
two cDNAs were dissimilar, although both mRNAs have potential for
significant secondary structure. The PEPCK-M mRNA contained several
G-C-rich regions which demonstrated free energies of formation in dyad
symmetry programs up to -70 kcal/mol. The 1.6-kilobase (kb) 3'-untranslated
region contained several repeat elements including one of 11 base pairs,
which was present 30 times; but, a signal sequence for polyadenylation was
not present. Each of the three PEPCK-M cDNA clones recognized two mRNAs of
4.2 and 3.4 kb in the livers and kidneys of starved or normally fed
chickens. However, the level of these two related PEPCK-M mRNAs changed in
response to cAMP treatment, with the larger mRNA predominant at 20 and 160
min and the 3.4-kb mRNA present at intermediate times. In contrast, the
level of the 2.8-kb PEPCK-C mRNA increased dramatically upon addition of
the cyclic nucleotide, particularly in the liver where it was not detected
without cAMP induction. Thus, PEPCK-M and PEPCK-C, clearly represented the
products of two distinct genes, which were distinguished by altered protein
sequences and non-cross-hybridizing, differentially regulated mRNAs.
Mitochondrial phosphoenolpyruvate carboxykinase from the chicken. Comparison of the cDNA and protein sequences with the cytosolic isozyme
Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
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