How Protein Structure and Expression Levels Affect Evolution Rates
Author Information
Author(s): Maxim Y Wolf, Yuri I Wolf, Eugene V Koonin
Primary Institution: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
Hypothesis
The rate of protein sequence evolution is influenced by both structural-functional constraints and gene expression levels.
Conclusion
The fusion of domains in multidomain proteins leads to a significant homogenization of evolutionary rates, but notable differences between domain-specific rates persist.
Supporting Evidence
- Highly expressed proteins evolve slower than lowly expressed ones.
- Fusion of domains leads to closer evolutionary rates within multidomain proteins.
- Significant differences in evolutionary rates remain between different domains.
Takeaway
This study shows that how fast proteins evolve depends on both their structure and how much they are made in the cell.
Methodology
A genome-wide analysis comparing evolutionary rates of protein domains in multidomain proteins versus those in separate proteins.
Potential Biases
Potential bias due to the assumption that all domains within multidomain proteins are expressed at the same rate.
Limitations
The study may not account for all extrinsic factors influencing evolutionary rates.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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