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Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

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Dimerization induces bimodality in protein number distributions.

Ming-Yang Ling¹, Lin-Jie Chiu¹, Ching-Chu Hsieh¹

¹Department of Chemical Engineering and Biotechnology, National Taipei University of Technology, Taipei City, Taiwan.

|November 25, 2022

Summary

Gene expression bimodality arises from protein dimerization, not transcriptional noise. DNA switching dynamics and protein degradation rates influence this emergent cell state switching.

Keywords:

Bistable toggle switches Mathematic model Transition probability

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Area of Science:

Molecular Biology
Systems Biology
Biophysics

Background:

Gene expression can exhibit subpopulations, but the underlying mechanisms are complex.
Transcriptional heterogeneity alone does not fully explain observed protein level bimodality.
Understanding emergent cell states is crucial for fields like developmental biology and disease research.

Purpose of the Study:

To investigate the mechanisms driving protein bimodality in gene expression.
To determine the role of protein dimerization and DNA switching in cell state emergence.
To explore the impact of varying degradation rates and dimerization constants on system dynamics.

Main Methods:

Utilized the Stochastic Simulation Algorithm (SSA) to model gene expression dynamics.
Analyzed RNA and protein distributions, including monomer and dimer forms.
Performed parameter sweeps to assess the influence of dimerization and DNA switching.

Main Results:

Protein bimodality emerges from protein monomer-dimer interplay, not transcriptional heterogeneity.
Decreasing dimerization rate constants significantly reduces or eliminates bimodality.
A specific ratio of active to inactive DNA states is necessary for bimodality.
Tetramerization of dimers also contributes to bimodality.

Conclusions:

Protein dimerization is a key driver of emergent cell state bimodality.
DNA switching dynamics play a critical role in establishing these distinct cell states.
The system exhibits spontaneous state switching at the protein level without deterministic bistability.