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Title: MOLECULAR CLONING AND CHARACTERIZATION OF A CDNA ENCODING CYTOCHROME C OXIDASE SUBUNIT VA FROM THE LESSER GRAIN BORER, RHYZOPERTHA DOMINICA (F.) (COLEOPTERA BOSTRICHIDAE)

Author
item AYALA, JORGE - KANSAS STATE UNIV
item DOWDY, ALAN - USDA APHIS
item Beeman, Richard
item ZHU, KUN - KANSAS STATE UNIV

Submitted to: Insect Biochemistry and Molecular Biology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/19/2003
Publication Date: 9/1/2003
Citation: AYALA, J., DOWDY, A.K., BEEMAN, R.W., ZHU, K.Y. MOLECULAR CLONING AND CHARACTERIZATION OF A CDNA ENCODING CYTOCHROME C OXIDASE SUBUNIT VA FROM THE LESSER GRAIN BORER, RHYZOPERTHA DOMINICA (F.) (COLEOPTERA BOSTRICHIDAE). INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY 54: 47-54. 2003.

Interpretive Summary: Cytochrome c oxidase is a target enyzme of phosphine, an insecticidal fumigant widely used to control stored grain insect pests. Phosphine resistance is becoming a serious problem in some areas of the world. We cloned and characterized a cytochrome c oxidase from lesser grain borer in order to better understand mechanisms of phosphine toxicity and resistance. Studies such as these will lead to better understanding of fumigant action and better strategies for minimizing the problem of resistance.

Technical Abstract: A cDNA encoding subunit Va of cytochrome c oxidase was cloned and characterized from a lesser grain borer (Rhyzopertha dominica) cDNA library. The complete cDNA consists of 693-bp and contains an open reading frame of 450-bp which encodes 150 amino acid residues. The sequence includes a 28-bp putative N-terminal and a 122-bp putative mature protein. The estimated molecular weight and pI for the predicted mature protein are 13,962 and 4.60, respectively. The cDNA-deduced amino acid sequence of the mature protein shows 73% identity to that of a corresponding subunit of African malaria mosquito (Anopheles gambiae) and 59% identity to that of the fruit fly (Drosophila melanogaster). In addition, 31% of all amino acid residues are conserved among six different animal species. Evolutionary distance analysis suggests that cytochrome c oxidase subunit Va from R. dominica is most similar to the corresponding subunit from the malaria mosquito. Northern analysis revealed a single 4.9-kb transcript that is much larger than that found in mammalian species. This enzyme is believed to be involved in phosphine toxicity and could also be involved in phosphine resistance mechanisms.