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Ryo Kurahashi1, Shun-Ichi Tanaka1, Kazufumi Takano1

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Summary

Protein evolvability correlates with parental stability, suggesting stability is crucial. Maximum activity increase from mutations conflicts with stability, revealing an activity-stability trade-off in protein evolution.

Keywords:
Directed evolutionEsteraseFitness landscapeHyperthermophilic archaeonSulfolobus tokodaii

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Previous studies linked protein evolvability to parental stability in esterase evolution.
  • Protein evolution must consider stability for meaningful advancement.

Purpose of the Study:

  • To evaluate the relationship between activity and stability in random protein mutations.
  • To introduce and compute a novel criterion, robustizability (stabilizability).
  • To explore the application of activity-stability trade-offs in directed evolution.

Main Methods:

  • Analysis of random mutational drift data from an esterase of Sulfolobus tokodaii.
  • Calculation of evolvability and robustizability from mutant libraries.
  • Correlation analysis between parental properties and variant outcomes.

Main Results:

  • High parental stability yielded many activated variants, but lower stability produced fewer, highly active variants.
  • Robustizability (stabilizability) positively correlated with parental activity and negatively with parental stability.
  • The activity-stability trade-off principle was evident even in random mutations.

Conclusions:

  • The study confirms the dominance of the activity-stability trade-off in protein evolution, even under random mutation.
  • Robustizability offers a new metric for assessing protein stability.
  • Stability selection is proposed as a key strategy for protein engineering via directed evolution.