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Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.

Zámocký M, Gasselhuber B, Furtmüller PG, Obinger C - Cell. Mol. Life Sci. (2014)

Bottom Line: In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain.Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily.We present and discuss their phylogeny, sequence signatures and putative biological function.

View Article: PubMed Central - PubMed

Affiliation: Division of Biochemistry, Department of Chemistry, VIBT, Vienna Institute of BioTechnology, BOKU, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria, marcel.zamocky@boku.ac.at.

ABSTRACT
Heme peroxidases and catalases are key enzymes of hydrogen peroxide metabolism and signaling. Here, the reconstruction of the molecular evolution of the peroxidase-catalase superfamily (annotated in pfam as PF00141) based on experimentally verified as well as numerous newly available genomic sequences is presented. The robust phylogenetic tree of this large enzyme superfamily was obtained from 490 full-length protein sequences. Besides already well-known families of heme b peroxidases arranged in three main structural classes, completely new (hybrid type) peroxidase families are described being located at the border of these classes as well as forming (so far missing) links between them. Hybrid-type A peroxidases represent a minor eukaryotic subfamily from Excavates, Stramenopiles and Rhizaria sharing enzymatic and structural features of ascorbate and cytochrome c peroxidases. Hybrid-type B peroxidases are shown to be spread exclusively among various fungi and evolved in parallel with peroxidases in land plants. In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain. Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily. We present and discuss their phylogeny, sequence signatures and putative biological function.

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Related in: MedlinePlus

Details of phylogenetic tree (Fig. 1) of hybrid-type B peroxidases. Obtained bootstrap values are presented for ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Those sequences where mRNA was detected (EST database) are labeled in bold
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Fig7: Details of phylogenetic tree (Fig. 1) of hybrid-type B peroxidases. Obtained bootstrap values are presented for ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Those sequences where mRNA was detected (EST database) are labeled in bold

Mentions: Hybrid-type B peroxidases are found in all fungal phyla, predominantly in phytopathogens. Their evolution occurred parallel with that of Class III peroxidases of land plants. Up to seven distinct clades of hybrid-type B peroxidases (Figs. 1 and 7) can be distinguished. In the basal clade for the whole hybrid-type B subfamily an enzyme from the basidiomycete Trichosporon asahii is found, which is a yeast-like fungus commonly inhabiting soils. It was described as an opportunistic human pathogen [57].Fig. 7


Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.

Zámocký M, Gasselhuber B, Furtmüller PG, Obinger C - Cell. Mol. Life Sci. (2014)

Details of phylogenetic tree (Fig. 1) of hybrid-type B peroxidases. Obtained bootstrap values are presented for ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Those sequences where mRNA was detected (EST database) are labeled in bold
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4232752&req=5

Fig7: Details of phylogenetic tree (Fig. 1) of hybrid-type B peroxidases. Obtained bootstrap values are presented for ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Those sequences where mRNA was detected (EST database) are labeled in bold
Mentions: Hybrid-type B peroxidases are found in all fungal phyla, predominantly in phytopathogens. Their evolution occurred parallel with that of Class III peroxidases of land plants. Up to seven distinct clades of hybrid-type B peroxidases (Figs. 1 and 7) can be distinguished. In the basal clade for the whole hybrid-type B subfamily an enzyme from the basidiomycete Trichosporon asahii is found, which is a yeast-like fungus commonly inhabiting soils. It was described as an opportunistic human pathogen [57].Fig. 7

Bottom Line: In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain.Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily.We present and discuss their phylogeny, sequence signatures and putative biological function.

View Article: PubMed Central - PubMed

Affiliation: Division of Biochemistry, Department of Chemistry, VIBT, Vienna Institute of BioTechnology, BOKU, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria, marcel.zamocky@boku.ac.at.

ABSTRACT
Heme peroxidases and catalases are key enzymes of hydrogen peroxide metabolism and signaling. Here, the reconstruction of the molecular evolution of the peroxidase-catalase superfamily (annotated in pfam as PF00141) based on experimentally verified as well as numerous newly available genomic sequences is presented. The robust phylogenetic tree of this large enzyme superfamily was obtained from 490 full-length protein sequences. Besides already well-known families of heme b peroxidases arranged in three main structural classes, completely new (hybrid type) peroxidase families are described being located at the border of these classes as well as forming (so far missing) links between them. Hybrid-type A peroxidases represent a minor eukaryotic subfamily from Excavates, Stramenopiles and Rhizaria sharing enzymatic and structural features of ascorbate and cytochrome c peroxidases. Hybrid-type B peroxidases are shown to be spread exclusively among various fungi and evolved in parallel with peroxidases in land plants. In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain. Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily. We present and discuss their phylogeny, sequence signatures and putative biological function.

Show MeSH
Related in: MedlinePlus