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2.
Insect Mol Biol ; 15(2): 217-25, 2006 Apr.
Article in English | MEDLINE | ID: mdl-16640732

ABSTRACT

We determined the complete nucleotide sequences of the mitochondrial genome (mitogenome) of the Korean hairstreak, Coreana raphaelis (Lepidoptera: Lycaenidae). The entire mitochondrial DNA (mtDNA) molecule was 15,314 bp long. The C. raphaelis genes were in the same order and orientation as the completely sequenced mitogenomes of other lepidopteran species, except for the presence of an extra copy of tRNA(Ser)(AGN). High similarity in primary sequence and secondary structure between the two tandemly located copies of the tRNA(Ser)(AGN) suggest a recent duplication of an original single tRNA(Ser)(AGN). The DHU arm of the two copies of tRNA(Ser)(AGN) formed a simple loop as seen in many other metazoan mt tRNA(Ser)(AGN). The putative initiation codon for the C. raphaelis COI gene appears to be a tetranucleotide, TTAG, found commonly in the sequenced lepidopterans. ATPase8, ATPase6, ND4L and ND6 genes, which are next to another protein-coding gene at their 3' end all had the sequences potential to form a hairpin structure, suggesting the importance of such a structure for precise cleavage of the mature protein-coding genes.


Subject(s)
Butterflies/genetics , DNA, Mitochondrial , Genome, Insect , AT Rich Sequence , Animals , Base Sequence , Genes, rRNA , Molecular Sequence Data , Physical Chromosome Mapping , RNA, Transfer/chemistry , RNA, Transfer/genetics , Sequence Analysis, DNA
3.
Biomol Eng ; 16(6): 211-5, 2000 Jun.
Article in English | MEDLINE | ID: mdl-10894116

ABSTRACT

QM, a novel gene that was firstly isolated as a putative tumor suppressor gene from Wilms' tumor cell line. Although it is well known that the QM gene product plays an important role within the tumor cells, the precise role of QM in the non-tumor cells has remained elusive. With in this mind we isolated a cDNA encoding QM homologue from Bombyx mandarina to understand the function of QM. The 596 bp cDNA has an open reading frame of 219 amino acids and a predicted mol. wt. of 25 kDa. The protein has more than 88% amino acid sequence identity to the QM protein from Drosophila melanogaster. mRNA expression gradually increased from 1-2 days after egg laying to 2 days of finial instar, while very low expressions were detected for either the pupae and the moth stages. The organs, posterior/middle division of silkgland, midgut, fat body and malpighian tubes, also show relatively high mRNA expression levels, respectively. The high degree of conservation and expression of the B. mandarina QM homologous suggest that it has a selectively conserved amino acid sequence due, presumably, to an important biological role which is associated with pupae formation.


Subject(s)
Bombyx/genetics , Carrier Proteins/genetics , Ribosomal Proteins , Amino Acid Sequence , Animals , Base Sequence , Blotting, Northern , Bombyx/metabolism , Carrier Proteins/biosynthesis , Cloning, Molecular , DNA, Complementary , Gene Expression Regulation, Developmental/genetics , Molecular Sequence Data , Phylogeny , RNA, Messenger/analysis , Ribosomal Protein L10 , Sequence Homology, Amino Acid
4.
Genet Anal ; 15(6): 223-8, 1999 Dec 15.
Article in English | MEDLINE | ID: mdl-10609758

ABSTRACT

The phylogenetic relationships between Bombycidae (Bombyx mori and Bombyx mandarina) and Saturniidae (Antheraea yamamai and Antheraea pernyi) were investigated based on large and small mitochondiral rRNA genes. About 430 bp of four kinds of PCR-amplified fragments were sequenced and aligned. For the 16S rRNA gene, B. mori shared a 98, 87 and 86% sequence homology with B. mandarina, A. yamamai and A. pernyi, and for the 12S rRNA gene, B. mori shared a 99, 89 and 88% sequence homology with B. mandarina, A. yamamai and A. pernyi, respectively. DNA sequence data were also used for a phylogenetic analysis. All of the trees showed monophyly for both Bombycidae and Saturniidae. The monophyly confidence limits of these trees were estimated using bootstrapping tests and measured more than 99% for all trees for both Bombycidae and Saturniidae.


Subject(s)
Bombyx/classification , DNA, Mitochondrial/genetics , DNA, Ribosomal/genetics , Moths/classification , Animals , Base Sequence , Bombyx/genetics , Molecular Sequence Data , Moths/genetics , Phylogeny , Polymerase Chain Reaction , RNA, Ribosomal/genetics , RNA, Ribosomal, 16S/genetics , Sequence Alignment
5.
Biol Chem ; 380(12): 1455-9, 1999 Dec.
Article in English | MEDLINE | ID: mdl-10661875

ABSTRACT

We isolated a cDNA representing a message that was strongly induced by injection with E. coli in Bombyx mori. The 2160 bp cDNA has an open reading frame of 644 amino acids and the deduced product a predicted molecular mass of 71 kDa. The cDNA sequence shared high homology with the transferrins known so far, and its deduced peptide had unique features of transferrins, that is, sites of cystein residues and iron binding. We suggest that the B. mori transferrin plays an important role in the self-defense system.


Subject(s)
Bombyx/genetics , Transferrin/genetics , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA, Complementary , Escherichia coli/genetics , Molecular Sequence Data , Open Reading Frames , Sequence Homology, Amino Acid
6.
Biochem Biophys Res Commun ; 246(2): 388-92, 1998 May 19.
Article in English | MEDLINE | ID: mdl-9610369

ABSTRACT

We differentially screened a novel gene encoding a new antibacterial peptide from the immunized Bombyx mori cDNA library. The gene showed a similar structure to that of cecropin-family, encoding 59 amino acids including a putative leader peptide and mature peptide. The deduced peptide, named Enbocin, had conserved amino acid residues which have been known to play an important role in the antibacterial activities. Enbocin genomic sequence revealed that the transcription unit of Enbocin gene was about 1.2 kb, and the coding sequence was interrupted by an intron of 660 bases. Recombinant Enbocin, expressed under the control of the baculovirus polyhedrin promoter, demonstrated a broad range of antibacterial activities against gram positive and gram negative bacteria.


Subject(s)
Anti-Bacterial Agents/chemistry , Bombyx/genetics , Genes, Insect , Insect Proteins/genetics , Peptides/genetics , Amino Acid Sequence , Animals , Anti-Bacterial Agents/pharmacology , Base Sequence , Cloning, Molecular , DNA/genetics , DNA Primers/genetics , Escherichia coli/drug effects , Escherichia coli/ultrastructure , Gene Expression , Gram-Negative Bacteria/drug effects , Gram-Positive Bacteria/drug effects , Insect Proteins/pharmacology , Molecular Sequence Data , Peptides/pharmacology , Recombinant Proteins/genetics , Recombinant Proteins/pharmacology , Restriction Mapping
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