Cooperative stability renders protein complex formation more robust and controllable.
Kuan-Lun Hsu1, Hsueh-Chi S Yen1, Chen-Hsiang Yeang2
1Institute of Molecular Biology, Academia Sinica, 128 Academia Road, Section 2, Taipei, Taiwan.
Scientific Reports
|June 21, 2022
Summary
Cooperative stability in protein complex formation enhances robustness against synthesis rate variations. This mechanism, unlike controlled synthesis, offers balanced performance for biological systems and synthetic design.
Area of Science:
- Molecular Biology
- Systems Biology
- Biophysics
Background:
- Protein complexes are essential for biological functions.
- Accumulation of unassembled subunits can be detrimental, leading to cytotoxicity.
- Existing research primarily focuses on controlled synthesis, leaving cooperative stability underexplored.
Purpose of the Study:
- To investigate the role and impact of cooperative stability in protein complex formation.
- To compare the behavior of systems with and without cooperative stability under varying synthesis rates.
- To evaluate the performance of different regulatory circuits combining negative feedback and cooperative stability.
Main Methods:
- Development of quantitative models for heteromeric protein complexes.
- In silico experiments to analyze system behavior under parameter variations.
- Comparative analysis of circuits based on optimality, robustness, and controllability.
Main Results:
- Systems with cooperative stability demonstrate robustness against synthesis rate fluctuations, maintaining high complex/subunit ratios.
- Cooperative stability mitigates subunit supply limitations and improves responsiveness to subunit upregulation.
- A system with cooperative stability alone exhibited the most balanced performance across multiple characteristics.
Conclusions:
- Cooperative stability is a significant factor in natural protein complex formation, contributing to system robustness.
- This study provides theoretical insights and a design framework for synthetic biological systems involving protein complex assembly.
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