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Citation for Study 13985

Citation title: "Origin, evolution and classification of type-3 copper proteins: Lineage-specific gene expansions and losses across the Metazoa".

Study name: "Origin, evolution and classification of type-3 copper proteins: Lineage-specific gene expansions and losses across the Metazoa".

This study is part of submission 13985 (Status: Published).

Citation

Aguilera F., Mcdougall C., & Degnan B.M. 2013. Origin, evolution and classification of type-3 copper proteins: Lineage-specific gene expansions and losses across the Metazoa. BMC Evolutionary Biology, .

Authors

• Aguilera F. (submitter) +61-0415511441
• Mcdougall C.
• Degnan B.M.

Abstract

Background. Tyrosinases, tyrosinase-related proteins, catechol oxidases and hemocyanins comprise the type-3 copper protein family and are involved in a variety of biological processes, including pigment formation, innate immunity and oxygen transport, via the binding of dioxygen. This family is present in the three domains of life, however previous studies have largely focussed on specific metazoan and plant lineages and the origin and early evolution of the family is not well understood. Results. Here, we use genomic, phylogenetic and structural analyses to show that the ancestral type-3 copper protein was secreted (so-called α subclass). The gene encoding this protein underwent two duplication events, the first being prior to the divergence of the unikont eukaryotic lineages and the second being before the diversification of animals. The former duplication gave rise to a cytosolic form (β) and the latter to a membrane-bound form (γ). Structural comparisons reveal that the active site of α and γ forms are covered by aliphatic amino acids, however, the active site of the β form has a highly conserved aromatic residue covering the active site, resulting in differing enzymatic activities between β and α/γ forms. The subsequent evolution of this gene family in modern lineages of multicellular eukaryotes is typified by the loss of one or more of these three subclasses and the lineage-specific expansion of one or both of the remaining subclasses. Conclusions. The diversity of type-3 copper proteins in animals and other eukaryotes is consistent with two ancient gene duplication events leading to α, β and γ subclasses, followed by the differential loss and expansion of one or more of these subclasses in specific kingdoms and phyla, which in turn has led to lineage-specific structural and functional adaptations and constraints. Functionally-classified tyrosinases and hemocyanins are polyphyletic, because the oxygen-carrying hemocyanins in arthropods evolved from a β-subclass tyrosinase while hemocyanins in molluscs and urochordates evolved independently from an α-subclass tyrosinase. The tyrosinases do not form a monophyletic clade. Minor conformational changes at the active site of α, β and γ forms produce type-3 copper proteins with capacities to either carry oxygen (hemocyanins), oxidize diphenols (catechol oxidase) or o-hydroxylate monophenols (tyrosinases).

Keywords

Type-3 copper proteins, catechol oxidase, tyrosinase, tyrosinase-related protein, hemocyanin, gene expansion, gene loss

External links

• DOI: 10.1186/1471-2148-13-96
• Other URL: http://http://www.biomedcentral.com/1471-2148/13/96/abstract

About this resource

• Canonical resource URI: http://purl.org/phylo/treebase/phylows/study/TB2:S13985
• Other versions: Nexus NeXML
• Show BibTeX reference

  		@ARTICLE{TreeBASE2Ref21819,
  	 author = {Felipe  Aguilera and Carmel  McDougall and Bernard M Degnan},
  	 title = {Origin, evolution and classification of type-3 copper proteins: Lineage-specific gene expansions and losses across the Metazoa},
  	 year = {2013},
  	 keywords = {Type-3 copper proteins, catechol oxidase, tyrosinase, tyrosinase-related protein, hemocyanin, gene expansion, gene loss},
  	 doi = {10.1186/1471-2148-13-96},
  	 url = {http://http://www.biomedcentral.com/1471-2148/13/96/abstract},
  	 pmid = {},
  	 journal = {BMC Evolutionary Biology},
  	 volume = {},
  	 number = {},
  	 pages = {},
  	 abstract = {Background. Tyrosinases, tyrosinase-related proteins, catechol oxidases and hemocyanins comprise the type-3 copper protein family and are involved in a variety of biological processes, including pigment formation, innate immunity and oxygen transport, via the binding of dioxygen. This family is present in the three domains of life, however previous studies have largely focussed on specific metazoan and plant lineages and the origin and early evolution of the family is not well understood.
  
  Results. Here, we use genomic, phylogenetic and structural analyses to show that the ancestral type-3 copper protein was secreted (so-called α subclass). The gene encoding this protein underwent two duplication events, the first being prior to the divergence of the unikont eukaryotic lineages and the second being before the diversification of animals. The former duplication gave rise to a cytosolic form (β) and the latter to a membrane-bound form (γ). Structural comparisons reveal that the active site of α and γ forms are covered by aliphatic amino acids, however, the active site of the β form has a highly conserved aromatic residue covering the active site, resulting in differing enzymatic activities between β and α/γ forms. The subsequent evolution of this gene family in modern lineages of multicellular eukaryotes is typified by the loss of one or more of these three subclasses and the lineage-specific expansion of one or both of the remaining subclasses.
  
  Conclusions. The diversity of type-3 copper proteins in animals and other eukaryotes is consistent with two ancient gene duplication events leading to α, β and γ subclasses, followed by the differential loss and expansion of one or more of these subclasses in specific kingdoms and phyla, which in turn has led to lineage-specific structural and functional adaptations and constraints. Functionally-classified tyrosinases and hemocyanins are polyphyletic, because the oxygen-carrying hemocyanins in arthropods evolved from a β-subclass tyrosinase while hemocyanins in molluscs and urochordates evolved independently from an α-subclass tyrosinase. The tyrosinases do not form a monophyletic clade. Minor conformational changes at the active site of α, β and γ forms produce type-3 copper proteins with capacities to either carry oxygen (hemocyanins), oxidize diphenols (catechol oxidase) or o-hydroxylate monophenols (tyrosinases).
  }
  }
  		

• Show RIS reference

  		TY  - JOUR
  ID  - 21819
  AU  - Aguilera,Felipe 
  AU  - McDougall,Carmel 
  AU  - Degnan,Bernard M
  T1  - Origin, evolution and classification of type-3 copper proteins: Lineage-specific gene expansions and losses across the Metazoa
  PY  - 2013
  KW  - Type-3 copper proteins
  KW  - catechol oxidase
  KW  - tyrosinase
  KW  - tyrosinase-related protein
  KW  - hemocyanin
  KW  - gene expansion
  KW  - gene loss
  UR  - http://http://www.biomedcentral.com/1471-2148/13/96/abstract
  N2  - Background. Tyrosinases, tyrosinase-related proteins, catechol oxidases and hemocyanins comprise the type-3 copper protein family and are involved in a variety of biological processes, including pigment formation, innate immunity and oxygen transport, via the binding of dioxygen. This family is present in the three domains of life, however previous studies have largely focussed on specific metazoan and plant lineages and the origin and early evolution of the family is not well understood.
  
  Results. Here, we use genomic, phylogenetic and structural analyses to show that the ancestral type-3 copper protein was secreted (so-called α subclass). The gene encoding this protein underwent two duplication events, the first being prior to the divergence of the unikont eukaryotic lineages and the second being before the diversification of animals. The former duplication gave rise to a cytosolic form (β) and the latter to a membrane-bound form (γ). Structural comparisons reveal that the active site of α and γ forms are covered by aliphatic amino acids, however, the active site of the β form has a highly conserved aromatic residue covering the active site, resulting in differing enzymatic activities between β and α/γ forms. The subsequent evolution of this gene family in modern lineages of multicellular eukaryotes is typified by the loss of one or more of these three subclasses and the lineage-specific expansion of one or both of the remaining subclasses.
  
  Conclusions. The diversity of type-3 copper proteins in animals and other eukaryotes is consistent with two ancient gene duplication events leading to α, β and γ subclasses, followed by the differential loss and expansion of one or more of these subclasses in specific kingdoms and phyla, which in turn has led to lineage-specific structural and functional adaptations and constraints. Functionally-classified tyrosinases and hemocyanins are polyphyletic, because the oxygen-carrying hemocyanins in arthropods evolved from a β-subclass tyrosinase while hemocyanins in molluscs and urochordates evolved independently from an α-subclass tyrosinase. The tyrosinases do not form a monophyletic clade. Minor conformational changes at the active site of α, β and γ forms produce type-3 copper proteins with capacities to either carry oxygen (hemocyanins), oxidize diphenols (catechol oxidase) or o-hydroxylate monophenols (tyrosinases).
  
  L3  - 10.1186/1471-2148-13-96
  JF  - BMC Evolutionary Biology
  VL  - 
  IS  - 
  ER  -