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The seminal work of Ohno in 1970 popularized the idea of gene duplication and divergence. DNA sequence comparison studies reveal that a large portion of the genes in bacteria, archaebacteria, and eukaryotes was  generated by gene duplication and divergence, indicating its critical role in evolution.
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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[Multinuclear blue copper-proteins: the evolutionary design].

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    Multinuclear blue copper-proteins (MBCP) evolved from simpler precursors through gene amplification and domain combination. These widespread proteins, including oxidases and reductases, showcase diverse evolutionary adaptations.

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    Area of Science:

    • Biochemistry and Molecular Evolution
    • Bioinorganic Chemistry

    Context:

    • Multinuclear blue copper-proteins (MBCP) are ubiquitous in nature, found in archaea, bacteria, and eukaryotes.
    • These proteins exhibit diverse functions, encompassing roles as oxidases, reductases, and crucial blood coagulation factors (V and VIII).

    Purpose:

    • To review the evolutionary pathways and mechanisms that have shaped multinuclear blue copper-proteins (MBCP).
    • To explore the structural and functional diversification of MBCP from a common protein precursor.

    Summary:

    • MBCP likely originated from a low-molecular weight, cupredoxin-like precursor.
    • Evolutionary mechanisms include gene amplification, domain shuffling, alterations in domain size, and modifications of copper-binding centers.
    • Further diversification involves changes in amino acid ligands, acquisition of other binding sites, and glycosylation.

    Impact:

    • Provides insights into the evolutionary strategies driving protein complexity and functional diversity.
    • Highlights the conserved yet adaptable nature of copper-binding proteins across different life forms.
    • Establishes a framework for understanding the structure-function relationships in MBCP.