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Positive selection for colicin diversity in bacteria

¹Department of Biology, Yale University, New Haven, Connecticut 06511.

Molecular Biology and Evolution

|September 1, 1993

Summary

Colicin proteins, particularly their immunity regions, evolve rapidly due to diversity-enhancing selection. This rapid evolution in Escherichia coli may be driven by recombination and positive selection.

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Area of Science:

Microbial genomics
Evolutionary biology
Bacterial genetics

Background:

Colicins are bacteriocins produced by Escherichia coli.
Colicin production provides a competitive advantage.
Colicin clusters include genes for the colicin toxin, immunity protein, and lysis.

Purpose of the Study:

To investigate diversity-enhancing selection acting on colicin proteins.
To analyze nucleotide substitution rates in colicin gene clusters.

Main Methods:

Studied synonymous, nonsynonymous, and intergenic nucleotide substitution rates.
Focused on three pairs of closely related colicin clusters.
Compared substitution rates between different regions of the colicin cluster.

Main Results:

The immunity gene and immunity-binding domain showed significantly higher substitution rates.
These regions accumulated synonymous and nonsynonymous substitutions several times faster than other parts of the colicin cluster.
Evidence suggests rapid divergence centered on the immunity protein.

Conclusions:

Colicin immunity regions are under strong positive selection.
Recombination and positive selection likely drive colicin diversity in natural populations.
This rapid evolution enhances bacterial adaptation and competition.

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