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First published online April 20, 2007
Journal of Experimental Biology 210, 1653-1660 (2007)
Published by The Company of Biologists 2007
doi: 10.1242/jeb.02725
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Evolvability of physiological and biochemical traits: evolutionary mechanisms including and beyond single-nucleotide mutation

Martin E. Feder

Department of Organismal Biology and Anatomy and The Committees on Evolutionary Biology, Genetics, and Molecular Medicine, The University of Chicago, 1027 E. 57th Street, Chicago, IL 60637, USA


Figure 1
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Fig. 1. Homage to Sidney Harris (Harris, 1992Go). The projected image exemplifies a common attitude of biologists towards natural selection; their focus is on how adapted organisms function rather than on how adaptations have arisen. © Alison Feder, used with permission.

 

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Fig. 2. Duplication–degeneration/complementation model of Force, Lynch, and colleagues (e.g. Force et al., 2005Go; Force et al., 1999Go). (A) After duplication, if one duplicate retains the original function, the other may either evolve a new function or deteriorate. (B) After duplication of a gene or module with multiple functions, the duplicates may each evolve distinct functions as long as each function of the ancestral gene/module continues.

 

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Fig. 3. Selection can purge standing variation from a population, and evolutionary capacitors can maintain it. Suppose alleles encoding `red' or `yellow' proteins, which fold differently to yield corresponding colors, segregate in an ancestral population. (A) In a yellow environment, conspicuousness to predators will soon eliminate the red allele from the population. (B) In a red environment, conspicuousness to predators will soon eliminate the yellow allele from a population. (C) If selection eliminates the red allele in the population in Environment A and this population then encounters the red environment, pre-existing variation may be insufficient for natural selection. The population may become extinct unless new variation arises. (D) An exemplary putative evolutionary capacitor, the molecular chaperone Hsp90 (CHAP), results in the folding of the red protein so that its conformation is the same as the yellow protein, yielding a yellow phenotype. Because the red phenotype is not expressed, genetic variation persists even in the yellow environment. (E) If the environment then becomes red and heat stress ensues, damaged proteins will out-compete the red proteins for chaperone, allowing the red proteins to fold to yield the red phenotype, which is beneficial in this environment. Compare the outcome here with that in C.

 





© The Company of Biologists Ltd 2007