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Comparative Study
. 2006 Oct;15(5):687-701.
doi: 10.1111/j.1365-2583.2006.00695.x.

Genes of the antioxidant system of the honey bee: annotation and phylogeny

M Corona  1 , G E Robinson
Affiliations
Comparative Study

Genes of the antioxidant system of the honey bee: annotation and phylogeny

M Corona et al. Insect Mol Biol. 2006 Oct.

Abstract

Antioxidant enzymes perform a variety of vital functions including the reduction of life-shortening oxidative damage. We used the honey bee genome sequence to identify the major components of the honey bee antioxidant system. A comparative analysis of honey bee with Drosophila melanogaster and Anopheles gambiae shows that although the basic components of the antioxidant system are conserved, there are important species differences in the number of paralogs. These include the duplication of thioredoxin reductase and the expansion of the thioredoxin family in fly; lack of expansion of the Theta, Delta and Omega GST classes in bee and no expansion of the Sigma class in dipteran species. The differential expansion of antioxidant gene families among honey bees and dipteran species might reflect the marked differences in life history and ecological niches between social and solitary species.

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Figures

Figure 1
Figure 1
Neighbour joining tree showing the relationships of the CuZn SOD family. The GenBank accession number (Anopheles gambiae), Flybase ID (Drosophila melanogaster) and BeeBase ID (Apis mellifera) are shown for each sequence. Values above the branches represent bootstrap support.
Figure 3
Figure 3
Neighbour joining tree showing the phylogenetic relationships of Apis mellifera (Am), Anopheles gambiae (Ag), Drosophila melanogaster (Dm) and Homo sapiens (Hs) peroxidases homologs. (A) Thioredoxin family. (B) Glutathione peroxidase homologs. Values above the branches represent bootstrap support.
Figure 2
Figure 2
Apis mellifera and Drosophila melanogaster thioredoxin-dependent peroxidase homologs. (A) Thioredoxin peroxidase family (peroxiredoxins). Predicted signal peptide for Dm Tpx-2 (Dpx4156) and mitochondrial targeting peptide of AmTpx3 and DmTpx-3 (Dpx5037) are underlined. Asterisks mark the peroxiredoxin domain. Conserved cysteins are highlighted. (B) Glutathione peroxidase homologs with thioredoxin peroxidase activity. Predicted signal peptides (AmGtpx2, DmGtpx1C) and mitochondrial targeting peptides (DmGtpx1D) are shown underlined. Amino acids of the catalytic site (Ursini et al., 1995) are highlighted. Amino acid colour follows the ClustalW code.
Figure 4
Figure 4
Alignments for thioredoxin reductases and thioredoxins from Apis mellifera (Am), Drosophila melanogaster (Dm) and Anopheles gambiae (Ag). (A) Thioredoxin reductase family. The sequences of redox-active centres are highlighted. (B) Fragment of an alignment of thioredoxin family proteins. The conserved active site (CXXC) (Holmgren, 1989) is highlighted.
Figure 5
Figure 5
Phylogenetic tree of the thioredoxin/glutharedoxin protein family. ‘M’ and ‘N’ after the accession number indicate mitochondrial or nuclear predicted subcellular localization. Values above the branches represent bootstrap support.
Figure 6
Figure 6
Phylogenetic relationships of GST family. GSTs belonging to the unclassified (Ding et al., 2003) class were not included. Values above the branches represent bootstrap support. Each entry has a species name (Am, for A. mellifera; Ag, for A. gambiae; Dm, for D. melanogaster), GST class, number if assigned, and accession number.
Figure 7
Figure 7
Intron position in Apis mellifera GST family members. With the exception of the third intron of GstS2, intron positions are conserved between the members of the Gst Sigma class. GstO2 genomic sequences is truncated toward the deduced C terminal region.
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