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Structural evolution of an amphibian-specific globin: A computational evolutionary biochemistry approach
João Pedro Fernandes Queiroz1, Marcos Roberto Lourenzoni2, Bruno Anderson Matias Rocha1
1Laboratorio de Biocristalografia - LABIC, Departamento de Bioquimica e Biologia Molecular, Universidade Federal do Ceara, Campus do Pici s.n., bloco 907, Av. Mister Hull, Fortaleza, Ceara, 60440-970, Brazil.
The amphibian-specific globin A (GbA) evolved from an alpha-globin precursor. Studies reveal the loss of its ancestral homodimeric state is common in the GbA clade due to genetic changes.
Area of Science:
- Evolutionary biology
- Molecular evolution
- Structural bioinformatics
Background:
- The globin gene family offers insights into protein evolution.
- A novel amphibian-specific globin A (GbA) arose from an alpha-globin precursor in Pelobatoidea and Neobatrachia.
- GbA in Rana catesbeiana is monomeric, unlike the ancestral alpha-globin homodimeric state.
Purpose of the Study:
- Investigate the genetic and physical mechanisms behind the origin of new protein properties.
- Determine the prevalence of the loss of the homodimeric state within the GbA clade.
- Characterize GbA gene loci in Bufo bufo.
Main Methods:
- Computational molecular evolution analyses.
- Structural bioinformatics.
- Gene locus characterization in Bufonidae species.
Main Results:
- Identified two GbA clades in Neobatrachia.
- Observed GbA deletion in Ranidae, but retention and expansion in Bufonidae.
- Found pervasive loss of the ancestral homodimeric state across the GbA clade.
Conclusions:
- Loss of GbA oligomerization is linked to amino acid substitutions in Pelobatoidea and independent deletions in Neobatrachia.
- Further taxonomic sampling is needed to ascertain the ancestral GbA oligomeric state.
- Independent genetic events led to the loss of homodimerization in different GbA lineages.
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