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Published on: August 28, 2019
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Stochastic protein multimerization, activity, and fitness.
Kyle Hagner1, Sima Setayeshgar1, Michael Lynch2
1Department of Physics, Indiana University, Bloomington, Indiana 47405, USA.
Physical Review. E
|June 20, 2019
Summary
Protein abundance influences homomultimeric protein structures. This study links protein quaternary structure to biochemical rates, revealing context-dependent benefits of protein multimerization for evolutionary diversification.
Area of Science:
- Biochemistry and Molecular Biology
- Evolutionary Biology
- Systems Biology
Background:
- Homomultimeric proteins assemble with varying subunit numbers across lineages.
- Protein abundance, influenced by gene expression and degradation rates, may explain structural variations.
- Cellular processes like growth and division also impact protein assembly.
Purpose of the Study:
- To develop a predictive framework linking protein quaternary structure to cellular biochemical rates.
- To investigate the functional role and evolutionary impact of protein multimerization.
- To explore how interface-binding energy influences multimer formation and stability.
Main Methods:
- Utilized a stochastic framework to model the multimeric state of proteins.
- Integrated parameters including mRNA and protein production/decay rates, cell growth/division rates, and binding free energy.
- Validated predictions using proteome data from *E. coli*.
Main Results:
- The model successfully predicted the multimeric state for a broad range of proteins.
- Demonstrated agreement between predicted and observed protein quaternary structures.
- Identified context-dependent benefits of multimerization, such as enhanced stability and catalytic efficiency.
Conclusions:
- The developed platform connects protein structure to gene expression and cellular dynamics.
- This framework can be extended to study the evolution and diversification of protein multimers.
- Multimerization offers fitness benefits that vary across different evolutionary lineages and cellular contexts.
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