Abstract
Many enzymes in intermediary metabolism manifest saturation kinetics in which flux is a concave function of enzyme activity and often of the Michaelis-Menten form. The result is that, when natural selection favors increased enzyme activity so as to maximize flux, a point of diminishing returns will be attained in which any increase in flux results in a disproportionately small increase in fitness. Enzyme activity ultimately will reach a level at which the favorable effect of an increase in activity is of the order 1/(4Ne) or smaller, where Ne is the effective population number. At this point, many mutations that result in small changes in activity will result in negligible changes in fitness and will be selectively nearly neutral. We propose that this process is a mechanism whereby conditions for the occurrence of nearly neutral mutations and gene substitutions can be brought about by the long-continued action of natural selection. Evidence for the hypothesis derives from metabolic theory, direct studies of flux, studies of null and other types of alleles in Drosophila melanogaster and chemostat studies in Escherichia coli. Limitations and complications of the theory include changes in environment or genetic background, enzymes with sharply defined optima of activity, overdominance, pleiotropy, multifunctional enzymes and branched metabolic pathways. We conclude that the theory is a useful synthesis that unites many seemingly unrelated observations. The principal theoretical conclusion is that the conditions for the occurrence of neutral evolution can be brought about as an indirect result of the action of natural selection.
MeSH Terms
Adaptation, Physiological
Alleles
Animals
Biological Evolution
Drosophila melanogaster/genetics
Enzymes/metabolism
Gene Frequency
Models, Genetic
Selection, Genetic
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hartl D L
Dykhuizen D E
Dean A M
References (15)
15 references, click to expand
-
Selection at the alcoholdehydrogenase locus in Drosophila melanogaster.
Experientia. 1975 Apr 15;31(4):418-20
PMID: 804412
-
The Genetic Structure of Natural Populations of DROSOPHILA MELANOGASTER. Xvi. Excess of Additive Genetic Variance of Viability.
Genetics. 1983 Sep;105(1):115-34
PMID: 17246151
-
Control of the flux in the arginine pathway of Neurospora crassa. Modulations of enzyme activity and concentration.
Biochem J. 1981 Nov 15;200(2):231-46
PMID: 6462136
-
Genetic diversity and structure in Escherichia coli populations.
Science. 1980 Oct 31;210(4469):545-7
PMID: 6999623
-
Null allele frequencies at allozyme loci in natural populations of Drosophila melanogaster.
Genetics. 1981 Sep;99(1):151-6
PMID: 6804301
-
Role of very slightly deleterious mutations in molecular evolution and polymorphism.
Theor Popul Biol. 1976 Dec;10(3):254-75
PMID: 1013905
-
Spontaneous and ethyl methanesulfonate-induced mutations controlling viability in Drosophila melanogaster. II. Homozygous effect of polygenic mutations.
Genetics. 1977 Nov;87(3):529-45
PMID: 200526
-
The alcohol dehydrogenase polymorphism in populations of Drosophila melanogaster. I. Selection in different environments.
Genetics. 1978 Sep;90(1):161-91
PMID: 100371
-
Species adaptation in a protein molecule.
Mol Biol Evol. 1983 Dec;1(1):1-28
PMID: 6400645
-
A general model to account for enzyme variation in natural populations. V. The SAS--CFF model.
Theor Popul Biol. 1978 Aug;14(1):1-45
PMID: 741392
-
Specific deletion occurring in the directed evolution of 6-phosphogluconate dehydrogenase in Escherichia coli.
Genetics. 1984 Dec;108(4):765-72
PMID: 6392014
-
Multilocus genetic structure in natural populations of Escherichia coli.
Proc Natl Acad Sci U S A. 1983 Mar;80(6):1751-5
PMID: 6340107
-
Mutation rate and dominance of genes affecting viability in Drosophila melanogaster.
Genetics. 1972 Oct;72(2):335-55
PMID: 4630587
-
Spontaneous Allozyme Mutations in DROSOPHILA MELANOGASTER: Rate of Occurrence and Nature of the Mutants.
Genetics. 1980 Apr;94(4):961-8
PMID: 17249027
-
Enzyme variation, metabolic flux and fitness: alcohol dehydrogenase in Drosophila melanogaster.
Genetics. 1983 Nov;105(3):633-50
PMID: 6416922