Molecular heterosis for heat-sensitive enzyme alleles.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 71 ·No. 5 ·1974-05-00 ·Pages 1808-10

Singh RS, Hubby JL, Lewontin RC

Abstract

Heat denaturation studies were carried out and revealed hidden genic variants with the same net charge at the Octanol dehydrogenase-1 locus in Drosophila pseudoobscura. Studies of several genetic crosses between strains with different heat-sensitivity alleles showed that the F(1) retained more in vitro enzyme activity after being heat-treated for a specified amount of time at a given temperature than the heat-resistant parent. We call this phenomenon "heterosis for heat-stability of enzyme activity" and discuss its possible molecular mechanism, its relation to maintenance of genetic variation in natural populations, and its bearing on the "classical" and "balance" hypotheses.

MeSH Terms

Alcohol Oxidoreductases Alleles Animals Chromosome Mapping Drosophila Electrophoresis Female Genetic Variation Heterozygote Hot Temperature Hybrid Vigor Hybridization, Genetic Male Octanols Time Factors

Chemicals

Octanols Alcohol Oxidoreductases

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Singh R S

Hubby J L

Lewontin R C

References (4)

4 references, click to expand

Electrophoretic variation in enzymes.
Science. 1965 Aug 27;149(3687):936-43 PMID: 5318249
A molecular approach to the study of genic heterozygosity in natural populations. IV. Patterns of genic variation in central, marginal and isolated populations of Drosophila pseudoobscura.
Genetics. 1969 Apr;61(4):841-58 PMID: 5364966
Isozyme specificity to temperature.
Nat New Biol. 1972 Sep 6;239(88):27-9 PMID: 4507333
Still more genetic variability in natural populations.
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3928-31 PMID: 4521219

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.71.5.1808

Published

1974-05-00

Pages

1808-10

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC388330

Subset

External Links

PubMed source DOI: 10.1073/pnas.71.5.1808 PMC Full Text View journal details

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