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Originally published In Press as doi:10.1074/jbc.M009576200 on December 7, 2000

J. Biol. Chem., Vol. 276, Issue 11, 7769-7774, March 16, 2001
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On a Potential Global Role for Vitamin K-dependent gamma -Carboxylation in Animal Systems
EVIDENCE FOR A gamma -GLUTAMYL CARBOXYLASE IN DROSOPHILA*

Craig S. WalkerDagger , Reshma P. ShettyDagger §, Kathleen ClarkDagger , Sandra G. Kazuko, Anthea Letsou, Baldomero M. OliveraDagger , and Pradip K. BandyopadhyayDagger ||

From the Departments of Dagger  Biology and  Human Genetics, University of Utah, Salt Lake City, Utah 84112-0840

The vitamin K-dependent gamma -carboxylation of glutamate to gamma -carboxyglutamate was originally well characterized in the mammalian blood clotting cascade. gamma -Carboxyglutamate 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 with mammalian gamma -carboxylase, which is 758 amino acids. The mammalian gene has 14 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 6 nucleotides is observed when cDNA and genomic sequences are compared. In situ hybridization to fixed embryos indicated ubiquitous presence of carboxylase mRNA throughout embryogenesis. Northern blot analysis revealed increased mRNA levels in 12-24-h embryos. The continued presence of carboxylase mRNA suggests that it plays an important role during embryogenesis. Although 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 suggest that this is a highly conserved and widely distributed post-translational modification in biological systems.

* This work was supported in part by a grant from the University of Utah Research Foundation (to P. K. B.), the Funding Initiative Seed Grant Program (1999), National Institutes of Health Grant GM48677, and Cognetix, Inc. (Salt Lake City, UT).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF170280.

§ Supported by a Pfizer summer undergraduate research fellowship and a Beckman undergraduate research fellowship.

|| To whom correspondence should be addressed: Dept. of Biology, University of Utah, 257 S. 1400 E., Rm. 201, Salt Lake City, UT 84112-0840. Tel.: 801-581-5907; Fax: 801-585-5010; E-mail: bandyop@biology.utah.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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