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Molecular cloning and characterization of a cDNA encoding cytochrome c oxidase subunit Va from the lesser grain borer, Rhyzopertha dominica (F.) (Coleoptera: Bostrichidae)
Author(s) -
Ayala Jorge,
Dowdy Alan K.,
Beeman Richard W.,
Zhu Kun Yan
Publication year - 2003
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.10101
Subject(s) - bostrichidae , biology , complementary dna , molecular cloning , protein subunit , cloning (programming) , oxidase test , cytochrome b , botany , microbiology and biotechnology , enzyme , biochemistry , gene , pest analysis , mitochondrial dna , computer science , programming language
A cDNA encoding subunit Va of cytochrome c oxidase (EC 1.9.3.1) 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 that 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. Arch. Insect Biochem. Physiol. 54:47–54, 2003. © 2003 Wiley‐Liss, Inc.