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The evolution of functionally novel proteins after gene duplication

¹Department of Biology, Pennsylvania State University, University Park 16802.

Proceedings. Biological Sciences

|May 23, 1994

Summary

The evolution of new protein functions doesn't rely on random mutations after gene duplication. Instead, gene sharing often precedes duplication, allowing specialization of ancestral gene functions.

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Area of Science:

Evolutionary biology
Molecular biology
Genetics

Background:

The mutation during non-functionality (MDN) model posits that gene duplication allows one copy to randomly acquire new functions.
This model suggests redundancy permits accumulation of neutral mutations, potentially leading to novel protein functions.
However, evidence challenges the premise of unconstrained mutation accumulation in duplicate genes.

Purpose of the Study:

To challenge the prevailing mutation during non-functionality (MDN) model for novel protein evolution.
To propose an alternative model emphasizing gene sharing and subsequent specialization.
To provide evidence supporting a revised understanding of protein evolution.

Main Methods:

Comparative analysis of expressed duplicate genes in Xenopus laevis.
Review of evidence from multi-gene families regarding selection pressures.
Examination of the phenomenon of gene sharing in protein evolution.

Main Results:

Expressed duplicate genes in Xenopus laevis are under purifying selection, contradicting random mutation accumulation.
Functionally distinct proteins often arise through positive Darwinian selection, not neutral drift.
Gene sharing demonstrates that new functions can evolve without prior gene duplication.

Conclusions:

The MDN model is contradicted by evidence of purifying selection on duplicate genes and positive selection for new functions.
Gene sharing is proposed as a precursor to functional divergence, with duplication facilitating specialization.
This revised model offers a more accurate framework for understanding the evolution of novel protein functions.

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