Molecular evolution of the zinc-containing long-chain alcohol dehydrogenase genes.
Open Access
- 1 March 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Molecular Biology and Evolution
- Vol. 7 (2) , 143-154
- https://doi.org/10.1093/oxfordjournals.molbev.a040593
Abstract
Phylogenetic relationships and rates of nucleotide substitution were studied for alcohol dehydrogenase (ADH) genes by using DNA sequences from mammals and plants. Mammalian ADH sequences include the three class I genes and a class II gene from humans and one gene each from baboon, rat, and mouse. Plant sequences include two ADH genes each from maize and rice, three genes from barley, and one gene each from wheat and two dicots, Arabidopsis and pea. Phylogenetic trees show that relationships among ADH genes are generally consistent with taxonomic relationships: mammalian and plant ADH genes are classified into two distinct groups; primate class I genes are clustered; and two dicot sequences are clustered separately from monocot sequences. Accelerated evolution has been detected among the duplicated ADH genes in plants, in which synonymous substitutions occurred more often within the coenzyme-binding domain than within the catalytic domains.This publication has 27 references indexed in Scilit:
- Human liver alcohol dehydrogenase. 2. The primary structure of the gamma1 protein chainEuropean Journal of Biochemistry, 1984
- Human liver alcohol dehydrogenase. 1. The primary structure of the beta1beta1 isoenzymeEuropean Journal of Biochemistry, 1984
- Estimation of evolutionary distance between nucleotide sequences.Molecular Biology and Evolution, 1984
- Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenaseProceedings of the National Academy of Sciences, 1983
- Further studies on the alcohol dehydrogenases in barley: evidence for a third alcohol dehydrogenase locus and data on the effect of an alcohol dehydrogenase – 1 null mutation in homozygous and in heterozygous conditionGenetics Research, 1983
- Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type.Proceedings of the National Academy of Sciences, 1981
- A MODEL OF EVOLUTIONARY BASE SUBSTITUTIONS AND ITS APPLICATION WITH SPECIAL REFERENCE TO RAPID CHANGE OF PSEUDOGENESGenetics, 1981
- Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein.Proceedings of the National Academy of Sciences, 1981
- Estimation of evolutionary distances between homologous nucleotide sequences.Proceedings of the National Academy of Sciences, 1981
- Evolution of Protein MoleculesPublished by Elsevier ,1969