Molecular Heterosis for Heat-Sensitive Enzyme Alleles | Zendy

Rama S. Singh | Zendy; J L Hubby | Zendy; Richard C Lewontin | Zendy

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Molecular Heterosis for Heat-Sensitive Enzyme Alleles

Author(s) -

Rama S. Singh,

J L Hubby,

Richard C Lewontin

Publication year - 1974

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.71.5.1808

Subject(s) - drosophila pseudoobscura , heterosis , allele , biology , genetics , locus (genetics) , enzyme , heat stability , mendelian inheritance , biochemistry , gene , hybrid , botany , materials science , composite material

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.

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