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On the evolutionary origin of the chaperonins
Carien Dekker1, Keith R Willison, William R Taylor
1Section of Cell and Molecular Biology, Chester Beatty Laboratories, Institute of Cancer Research, London, UK.
Proteins
|February 16, 2011
Summary
Chaperonins, essential protein folding machines, may have evolved from peroxiredoxins, not phosphotransferases. This structural analysis suggests a peroxiredoxin origin explains chaperonin function and interactions with other proteins.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Structural Biology
Background:
- Chaperonins are molecular machines crucial for protein folding.
- The apical domain of Group-I and Group-II chaperonins exhibits structural similarities to phosphotransferase and peroxiredoxin folds.
- Sequence similarity does not strongly support either evolutionary relationship.
Purpose of the Study:
- To investigate the evolutionary origin of the chaperonin apical domain.
- To compare the likelihood of phosphotransferase versus peroxiredoxin origins based on structural and evolutionary considerations.
- To explore functional implications of a potential peroxiredoxin ancestry.
Main Methods:
- Structural analysis of chaperonin apical domains.
- Comparison of structural similarities with phosphotransferase and peroxiredoxin folds.
- Evaluation of evolutionary pathways for domain acquisition.
Main Results:
- Structural similarity to both phosphotransferase and peroxiredoxin folds is weak.
- A peroxiredoxin origin requires a simpler evolutionary rearrangement (domain-swap) compared to a phosphotransferase origin (large insertion/deletion).
- Peroxiredoxins can form ring complexes with chaperone activity, mirroring chaperonin structure.
Conclusions:
- The peroxiredoxin fold is a plausible evolutionary precursor to the chaperonin apical domain.
- An insertion of a peroxiredoxin into an ancestral ATPase domain could explain the current chaperonin structure.
- This evolutionary hypothesis accounts for functional similarities and interactions with thioredoxin-fold proteins.
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