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Evolution based on domain combinations: the case of glutaredoxins
Rui Alves1, Ester Vilaprinyo, Albert Sorribas
1Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, IRBLleida, Lleida, Spain. ralves@cmb.udl.es
BMC Evolutionary Biology
|March 27, 2009
Summary
Glutaredoxin (GRX) domains evolved from a single ancestral gene in all organisms. However, a rare case of convergent evolution was found, where a thioredoxin (TRX) domain fused with a GRX domain twice independently.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Biochemistry
Background:
- Protein domains are fundamental units in protein evolution, primarily shaped by duplication, recombination, and fusion.
- Glutaredoxin (GRX) domains, found across archaea, bacteria, and eukaryotes, are crucial for redox regulation but their evolutionary paths are not fully understood.
Purpose of the Study:
- To investigate the distribution and evolutionary history of GRX proteins and domains across the tree of life.
- To explore the mechanisms driving the evolution of multidomain architectures involving GRX domains.
Main Methods:
- Analysis of over one thousand GRX proteins from diverse organisms.
- Tracing the evolutionary origin and diversification of the GRX domain.
Main Results:
- Single-domain GRX proteins (CGFS and CPYC classes) likely originated from a single ancestral gene present in the last common ancestor.
- Identified a unique instance of convergent evolution involving GRX domain architecture.
Conclusions:
- The evolution of GRX proteins primarily follows the dominant model of gene duplication and divergence.
- Convergent evolution, specifically two independent recombination events fusing a thioredoxin (TRX) domain to a GRX domain, represents a significant exception to established evolutionary mechanisms.
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