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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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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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Molecular Evolution of the Oxygen-Binding Hemerythrin Domain.

Claudia Alvarez-Carreño1, Arturo Becerra1, Antonio Lazcano1,2

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Hemerythrin, an ancient protein, evolved early in prokaryotes to bind oxygen and protect against oxidative damage. Its complex evolutionary history involves gene transfer and diversification across bacteria, archaea, and eukaryotes.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Genomics

Background:

  • Oxygenic photosynthesis drove the evolution of proteins that minimize reactive oxygen species damage.
  • Four protein families, including hemerythrin, independently evolved reversible oxygen-binding capabilities.
  • Hemerythrin's presence across all three domains of life suggests an ancient origin predating eukaryotes.

Purpose of the Study:

  • To investigate the evolutionary history and distribution of oxygen-binding hemerythrin.
  • To understand the functional diversification of hemerythrin domains in various organisms.

Main Methods:

  • Bioinformatic analysis of 367 bacterial, 21 archaeal, and 4 eukaryotic genomes for hemerythrin homologs.
  • Phylogenetic analysis using maximum-likelihood trees to reconstruct evolutionary relationships.
  • Classification of associated protein domains in long hemerythrin sequences.

Main Results:

  • Oxygen-binding hemerythrins form a monophyletic subgroup within the hemerythrin/HHE cation-binding domain.
  • Homologs were found across bacterial, archaeal, and eukaryotic genomes, indicating widespread distribution.
  • Hemerythrin domains are often integrated into signaling pathways, including signal transduction and phosphorelay response regulation.
  • Evolutionary history is complex, marked by lateral gene transfer, duplications, and gene losses.

Conclusions:

  • Hemerythrin is an ancient protein domain with a complex evolutionary trajectory.
  • Its iron-binding site originated in prokaryotes before the divergence of major bacterial phyla.
  • Hemerythrin spread widely and diversified in function, from oxidative stress protection to oxygen supply in aerobic and facultative species.