Comparative evolutionary analysis of protein complexes in E. coli and yeast.
Adam J Reid1, Juan Ag Ranea, Christine A Orengo
1Research Department of Structural & Molecular Biology, University College London, London, WC1E 6BT, UK. ar11@sanger.ac.uk
BMC Genomics
|February 4, 2010
Summary
Protein complex evolution differs significantly between E. coli and yeast. Yeast complexes utilize paralogs for eukaryotic-specific functions, a pattern less evident in E. coli, suggesting distinct evolutionary strategies for protein machinery.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Systems Biology
Background:
- Proteins function in complexes for cellular processes.
- The evolution of protein complexes is poorly understood, especially outside of yeast.
Purpose of the Study:
- To investigate differences in protein complex evolution between E. coli and yeast.
- To compare models of complex evolution in these two species.
Main Methods:
- Generated high-coverage protein complex datasets for E. coli and yeast.
- Analyzed homologous and non-homologous domain interactions within complexes.
Main Results:
- Significant differences in complex evolution were observed between E. coli and yeast.
- Yeast complexes show a greater reliance on paralogs and eukaryotic-specific functions.
- Correlated non-homologous domains were identified as potential complex cores in yeast, but not E. coli.
Conclusions:
- Protein complex evolution varies between E. coli and yeast.
- Yeast complex evolution involves recruiting paralogs for eukaryotic-specific functions.
- Homologous domains are generally utilized in different complexes across both species.
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