Opossum Hb chain sequence and neutral mutation theory

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

THE divergence of amino acid sequences which has accompanied evolution of species may be largely due to random fixation of selectively neutral or nearly neutral mutations. This was proposed by Kimura upon consideration of an inferred rapid rate of molecular evolution, the theory of the cost of natural selection, and observed high levels of polymorphism in natural populations1. Among the observations considered to favour the neutral mutation-random fixation theory1-4, the apparent uniformity of the rate of fixation of amino acid substitutions in homologous proteins along several phyletic lines is outstanding. Kimura proposed this test of the neutral mutation theory by examining the amino acid sequences of proteins from so-called 'living fossils'4. If, for a very long slowly evolving line, a rate of molecular evolution equal to that of more rapidly evolving lines is inferred (and it is assumed that the rate of evolution of physiological adaptations generally parallels the morphological evolutionary rate) then a case is made for the fixation of neutral mutations. The amino acid sequence proposed here 5 (Fig. 1) for the α chain of haemoglobin from a 'living fossil'6, Didelphis marsupialis, the Virginia opossum may be taken for such a test of the neutral mutation theory.

Original languageEnglish (US)
Pages (from-to)62-63
Number of pages2
JournalNature
Volume252
Issue number5478
DOIs
StatePublished - 1974
Externally publishedYes

Fingerprint

Opossums
Mutation
Amino Acid Sequence
Molecular Evolution
Didelphis
Physiological Adaptation
Genetic Selection
Amino Acid Substitution
Hemoglobins
Proteins
Costs and Cost Analysis

ASJC Scopus subject areas

  • General

Cite this

Opossum Hb chain sequence and neutral mutation theory. / Stenzel, Peter.

In: Nature, Vol. 252, No. 5478, 1974, p. 62-63.

Research output: Contribution to journalArticle

Stenzel, Peter. / Opossum Hb chain sequence and neutral mutation theory. In: Nature. 1974 ; Vol. 252, No. 5478. pp. 62-63.
@article{1b2461d2dac14494ae771642d7516cb8,
title = "Opossum Hb chain sequence and neutral mutation theory",
abstract = "THE divergence of amino acid sequences which has accompanied evolution of species may be largely due to random fixation of selectively neutral or nearly neutral mutations. This was proposed by Kimura upon consideration of an inferred rapid rate of molecular evolution, the theory of the cost of natural selection, and observed high levels of polymorphism in natural populations1. Among the observations considered to favour the neutral mutation-random fixation theory1-4, the apparent uniformity of the rate of fixation of amino acid substitutions in homologous proteins along several phyletic lines is outstanding. Kimura proposed this test of the neutral mutation theory by examining the amino acid sequences of proteins from so-called 'living fossils'4. If, for a very long slowly evolving line, a rate of molecular evolution equal to that of more rapidly evolving lines is inferred (and it is assumed that the rate of evolution of physiological adaptations generally parallels the morphological evolutionary rate) then a case is made for the fixation of neutral mutations. The amino acid sequence proposed here 5 (Fig. 1) for the α chain of haemoglobin from a 'living fossil'6, Didelphis marsupialis, the Virginia opossum may be taken for such a test of the neutral mutation theory.",
author = "Peter Stenzel",
year = "1974",
doi = "10.1038/252062a0",
language = "English (US)",
volume = "252",
pages = "62--63",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "5478",

}

TY - JOUR

T1 - Opossum Hb chain sequence and neutral mutation theory

AU - Stenzel, Peter

PY - 1974

Y1 - 1974

N2 - THE divergence of amino acid sequences which has accompanied evolution of species may be largely due to random fixation of selectively neutral or nearly neutral mutations. This was proposed by Kimura upon consideration of an inferred rapid rate of molecular evolution, the theory of the cost of natural selection, and observed high levels of polymorphism in natural populations1. Among the observations considered to favour the neutral mutation-random fixation theory1-4, the apparent uniformity of the rate of fixation of amino acid substitutions in homologous proteins along several phyletic lines is outstanding. Kimura proposed this test of the neutral mutation theory by examining the amino acid sequences of proteins from so-called 'living fossils'4. If, for a very long slowly evolving line, a rate of molecular evolution equal to that of more rapidly evolving lines is inferred (and it is assumed that the rate of evolution of physiological adaptations generally parallels the morphological evolutionary rate) then a case is made for the fixation of neutral mutations. The amino acid sequence proposed here 5 (Fig. 1) for the α chain of haemoglobin from a 'living fossil'6, Didelphis marsupialis, the Virginia opossum may be taken for such a test of the neutral mutation theory.

AB - THE divergence of amino acid sequences which has accompanied evolution of species may be largely due to random fixation of selectively neutral or nearly neutral mutations. This was proposed by Kimura upon consideration of an inferred rapid rate of molecular evolution, the theory of the cost of natural selection, and observed high levels of polymorphism in natural populations1. Among the observations considered to favour the neutral mutation-random fixation theory1-4, the apparent uniformity of the rate of fixation of amino acid substitutions in homologous proteins along several phyletic lines is outstanding. Kimura proposed this test of the neutral mutation theory by examining the amino acid sequences of proteins from so-called 'living fossils'4. If, for a very long slowly evolving line, a rate of molecular evolution equal to that of more rapidly evolving lines is inferred (and it is assumed that the rate of evolution of physiological adaptations generally parallels the morphological evolutionary rate) then a case is made for the fixation of neutral mutations. The amino acid sequence proposed here 5 (Fig. 1) for the α chain of haemoglobin from a 'living fossil'6, Didelphis marsupialis, the Virginia opossum may be taken for such a test of the neutral mutation theory.

UR - http://www.scopus.com/inward/record.url?scp=0016346219&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016346219&partnerID=8YFLogxK

U2 - 10.1038/252062a0

DO - 10.1038/252062a0

M3 - Article

VL - 252

SP - 62

EP - 63

JO - Nature

JF - Nature

SN - 0028-0836

IS - 5478

ER -