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Updated: Jul 14, 2026
04:52
Following the Dynamics of Structural Variants in Experimentally Evolved Populations
Published on: February 3, 2023
Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution.
Jesse D Bloom1, Philip A Romero, Zhongyi Lu
1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. jesse.bloom@gmail.com
Biology Direct
|June 30, 2007
Summary
Neutral mutations can significantly alter protein functions not under selection, potentially enabling future evolution. This study shows how genetic drift in cytochrome P450 enzymes can lead to major changes in promiscuous activities.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Engineering
Background:
- Many protein mutations are neutral to primary function.
- New functions evolve from selection on incidental, or promiscuous, activities.
- Neutral mutations impacting promiscuous functions may enable future evolution.
Purpose of the Study:
- Investigate if neutral mutations alter protein promiscuous functions.
- Examine changes in cytochrome P450 enzyme activities on multiple substrates.
- Assess the potential for future functional evolution.
Main Methods:
- Experimental evolution of cytochrome P450 enzymes.
- Assessed catalytic activity on six different substrates.
- Analyzed changes in promiscuous activities relative to mutation accumulation.
Main Results:
- Cytochrome P450 enzymes showed up to four-fold changes in promiscuous activities.
- Changes in promiscuous activities correlated with the number of mutations.
- Activity changes were rationalized by substrate chemical structures.
- Activities on similar substrates changed coordinately.
Conclusions:
- Neutral genetic drift can substantially alter non-selected protein functions.
- This alteration primes proteins for future functional evolution.
- Changes in promiscuous activities may be predictable based on substrate similarity.
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