Summary
Essential proteins are more likely to be thermostable (1) and over-expressed (2) than non-essential proteins. These results were obtained in E. coli and Acinetobacter baylyi, respectively. This points to varying degrees of evolutionary pressure being placed on proteins, depending on their impact on cellular fitness, and directly contradicts the principle of marginal thermostability.
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Ref (1)
Ref (2)
1.
Leuenberger P, Ganscha S, Kahraman A, Cappelletti V, Boersema PJ, von Mering C, et al. Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability. Science. 2017;355(6327). Available from: https://doi.org/10.1126/science.aai7825
2.
Choi HJ, Lo TW, Cutler KJ, Huang D, Will WR, Wiggins PA. Protein overabundance is driven by growth robustness. Science Advances. 2026;12(12). Available from: https://doi.org/10.1126/sciadv.adz9623