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A more recent version of this article appeared on March 9, 2001
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M009576200v1
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Papers In Press, published online ahead of print December 7, 2000
J. Biol. Chem, 10.1074/jbc.M009576200
Submitted on October 19, 2000
Revised on December 7, 2000
Accepted on December 6, 2000

On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems: Evidence for a gamma-glutamyl carboxylase in drosophila

Craig S. Walker, Reshma P. Shetty, Kathleen A. Clark, Sandra G. Kazuko, Anthea Letsou, Baldomero M. Olivera, and Pradip K. Bandyopadhyay

Department of Biology, University of Utah, Salt Lake City, Utah 84112-0840

Corresponding Author: bandyop{at}biology.utah.edu

SUMMARY The vitamin K-dependent gamma -carboxylation of glutamate to gamma -carboxyglutamate (Gla) was originally well characterized in the mammalian blood clotting cascade. Gla has also been found in a number of other mammalian proteins and in neuropeptides from the venoms of marine snails belonging to the genus Conus, suggesting wider prevalence of gamma -carboxylation. We demonstrate that an open reading frame from a Drosophila melanogaster cDNA clone encodes a protein with vitamin K-dependent gamma -carboxylase activity. The open reading frame, 670 amino acids in length, is truncated at the C-terminal end compared to mammalian g-carboxylase, which is 758 amino acids. The mammalian gene has fourteen introns; in Drosophila there are two much shorter introns, but in positions precisely homologous to two of the mammalian introns. In addition, a deletion of six nucleotides is observed when cDNA and genomic sequences are compared. In situ hybridization to fixed embryos indicate ubiquitous presence of carboxylase mRNA throughout embryogenesis. Northern blot analysis reveals increased mRNA levels in 12-24 hr embryos. The continued presence of carboxylase mRNA suggests that it plays an important role during embryogenesis. While the model substrate FLEEL is carboxylated by the enzyme, a substrate containing the propeptide of a Conus carboxylase substrate, conantokin G, is poorly carboxylated. Its occurrence in vertebrates, molluscan systems (i.e., Conus) and Drosophila, and the apparently strong homology between the three systems, suggests that this is a highly conserved and widely distributed post-translational modification in biological systems.


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