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Title: Cloning and molecular characterization of an ornithine cecarboxylase gene and its expression during embryonic eevelopment of the housefly, Musca domestica

Author
item Toutges, Michelle
item SANTOSO, ADI - North Dakota State University

Submitted to: Archives of Insect Biochemistry and Physiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/1/2010
Publication Date: 2/15/2011
Citation: Toutges, M.J., Santoso, A. 2011. Cloning and molecular characterization of an ornithine cecarboxylase gene and its expression during embryonic eevelopment of the housefly, Musca domestica. Archives of Insect Biochemistry and Physiology. 78(2): 87-103. http://dx.doi.org/10.1002/arch.20442.

Interpretive Summary: The house fly is a nuisance pest and a vector of disease for humans and many domestic animals. We are investigating new ways to control this pest by developing methods to interfere with its development. One possible target for control is ornithine decarboxylase (ODC), an enzyme involved in the regulation of polyamines, which are critical to many cell processes and to survival of all organisms studied to date. We cloned and sequenced the gene responsible for ODC production, and we characterized expression of the gene throughout development of the house fly egg. ODC expression and activity peak just prior to egg hatching indicating its importance in the transition from the egg to the larval stage. Improved understanding of ODC and its role in insect development will help us develop ODC as a new tool for insect pest management.

Technical Abstract: We are interested in identifying targets that may be used to develop new control products for the common house fly, Musca domestica, a vector of disease for many vertebrates. One such target, ornithine decarboxylase (ODC), is an embryonic enzyme involved in the regulation of polyamines and is a critical enzyme during M. domestica development. In this study, the cDNA for ODC from M. domestica was cloned, sequenced, and characterized. The full-length cDNA was 1,337-bp, consistent with a single band of approximately 1.35 kb obtained by northern analysis. The open-reading frame contains 1,191 bp, yielding a deduced polypeptide of 396 amino acid residues with a predicted mass of 44,618 Daltons. The deduced M. domestica ODC protein was homologous to other ODC proteins. mRNA expression profiles analyzed by real-time PCR indicated that the ODC transcript is temporally regulated throughout embryogenesis. Sequence data and Southern blot analysis suggests that there were likely only one or two closely-linked copies of the M. domestica ODC gene.