ADH Isozymes Research Articles

Regulated Expression of Three Alcohol Dehydrogenase Genes in Barley Aleurone Layers

Three genes specify alcohol dehydrogenase (EC 1.1.1.1.; ADH) enzymes in barley (Hordeum vulgare L.) (Adh 1, Adh 2, and Adh 3). Their polypeptide products (ADH 1, ADH 2, ADH 3) dimerize to give a total of six ADH isozymes which can be resolved by native gel electrophoresis and stained for enzyme activity.Under fully aerobic conditions, aleurone layers of cv Himalaya had a high titer of a single isozyme, the homodimer containing ADH 1 monomers. This isozyme was accumulated by the aleurone tissue during the later part of seed development, and survived seed drying and rehydration. The five other possible ADH isozymes were induced by O(2) deficit. The staining of these five isozymes on electrophoretic gels increased progressively in intensity as O(2) levels were reduced below 5%, and were most intense at 0% O(2).In vivo(35)S labeling and specific immunoprecipitation of ADH peptides, followed by isoelectric focusing of the ADH peptides in the presence of 8 molar urea (urea-IEF) demonstrated the following. (a) Aleurone layers incubated in air synthesized ADH 1 and a trace of ADH 2; immature layers from developing seeds behaved similarly. (b) At 5% O(2), synthesis of ADH 2 increased and ADH 3 appeared. (c) At 2% and 0% O(2), the synthesis of all three ADH peptides increased markedly.Cell-free translation of RNA isolated from aleurone layers, followed by immunoprecipitation and urea-IEF of in vitro synthesized ADH peptides, showed that levels of mRNA for all three ADH peptides rose sharply during 1 day of O(2) deprivation. Northern hybridizations with a maize Adh 2 cDNA clone established that the clone hybridized with barley mRNA comparable in size to maize Adh 2 mRNA, and that the level of this barley mRNA increased 15- to 20-fold after 1 day at 5% or 2% O(2), and about 100-fold after 1 day at 0% O(2).We conclude that in aleurone layers, expression of the three barley Adh genes is maximal in the absence of O(2), that regulation of mRNA level is likely to be a major controlling factor, and that whereas the ADH system of barley has strong similarities to that of maize, it also has some distinctive features.

ADH isozymes in seed of Nicotiana species and somatic hybrids

ADH isozymes in seed of Nicotiana species and somatic hybrids

Alcohol dehydrogenase isozymes in the clawed frog, Xenopus laevis

Alcohol dehydrogenase (ADH; EC 1.1.1.1) activity in Xenopus laevis was highest in liver tissue, with decreasing activities in kidney, heart, and gut tissues, respectively. Essentially no activity was found among other tissues screened, including lung, ovary, eye, and testes. Also, there was no apparent sexual dimorphism of ADH activity in either liver or kidney tissue. All ADH isozymes were inhibited by 10 mM pyrazole, and no eye-specific retinol dehydrogenase activity was detected on starch gel electropherograms. Isozyme patterns from 418 offspring from 11 different crosses could be explained genetically assuming the presence of two structural genes coding for ADH production: one carrying two electrophoretically separable variants and the other showing quantitative variation in its expression. The ADH system in X. laevis should be useful for studies concerning the molecular mechanisms governing the expression of ADH activity in vertebrate development.

Linkage of the alcohol dehydrogenase structural genes in pearl millet (Pennisetum typhoides).

Pearl millet produces three ADH isozymes, Sets I, II, and III. Naturally occurring ADH electrophoretic variants affecting Sets I and II isozymes but not III have been previously described. Analysis of such variants led to the identification of the Adh1 structural gene. The existence of a second Adh structural gene was inferred from dissociation-reassociation studies of Set II. In the present report, a naturally occurring variant affecting the electrophoretic mobility of Sets III and II but not Set I is described. Analysis of this variant confirms the existence of a second structural gene, Adh2. Crosses utilizing this Adh2 marker reveal a dissimilarity with maize and other plants such as sunflower and narrow-leafed lupins. Adh1 and Adh2 of pearl millet do not segregate independently; indeed, no recombinants have been observed. This is the first major difference encountered in an otherwise remarkably similar genetic and environmental control of the ADH isozymes in maize and millet. The organization of the Adh genes of pearl millet may reflect a more primitive arrangement than that of maize.

Natural variants of pearl millet (Pennisetum typhoides) with altered levels of set II alcohol dehydrogenase activity.

Two linked genes, Adh1 and Adh2, specify three sets of ADH isozymes in pearl millet. Set I is a homodimer specified by Adh1, Set III is a homodimer specified by Adh2, and Set II is a heterodimer consisting of one ADH1 subunit and one ADH2 subunit. Dry seeds exhibit only Sets I and II. Anaerobic treatment of seeds greatly increases the activity of Sets I and II and causes the Set III isozymes to be expressed. In the investigation reported here, the ADH zymogram phenotypes of 112 inbred pearl millet lines were analyzed. Two kinds of naturally occurring ADH variant strains were observed: in the "low-activity" variant, Set II activity is low in the dry seed, and no Set II activity is present upon anaerobic treatment. In the "high-activity" variant, Set II activity is high and Set III isozymes are expressed in the dry seed. The mutation in the high-activity strain appears to affect the product of Adh2 and not the product of Adh1. Dominance tests show that the mutations in both types of variant strains act in cis. These observations and linkage tests indicate that the mutations are closely linked to or at the Adh2 locus.

The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae: isolation, structure, and regulation.

Alcohol dehydrogenase (E.C. 1.1.1.1. ADH) catalyzes the inter-conversion of an alcohol and an aldehyde with NAD+ as a cofactor. In most higher organisms that have been studied, several different isozymes of ADH are present. The main function of these isozymes is presumed to be catabolic, to degrade various alcohols or sterols. This presumption is based primarily on the substrate preferences of the various isozymes and the absence of a fermentative pathway for alcohol production during glycolysis. In many organisms there is a distinctive tissue specificity in the distribution of different ADH isozymes.

Purification and properties of two distinct groups of ADH isozymes from Chinese hamster liver.

Two major classes of alcohol dehydrogenase isozymes have been purified from Chinese hamster liver. The two isozyme classes have the same subunit molecular weights but different electrophoretic mobilities. They have a similar range of substrates but different KROM values and sensitivities to the inhibitor pyrazole. The ADHs are immunologically related as determined by Ouchterlony double diffusion experiments. These results suggest that the isozymes are encoded by different structural gene loci derived from a common ancestral gene.

THE CYTOGENETIC LOCALIZATION OF THE ALCOHOL DEHYDROGENASE-1 LOCUS IN MAIZE

The alcohol dehydrogenase-1 (Adh) locus in maize has been positioned relative to thirteen reciprocal translocations that have breakpoints in the long arm of chromosome 1(1L). The methods of Gopinath and Burnham (1956) to produce interstitial segmental trisomy with overlapping translocations and of Rakha and Robertson (1970) to produce compound B-A translocations were coupled with the co-dominant nature of the ADH isozymes to allow the cytological placement. The results of several crosses are consistent with Adh being in the region of 0.80-0.90 of 1L.--The duplication that results from the overlap of translocations 1-3(5267) and 1-3(5242) and that includes Adh was studied with respect to meiotic segregation and pollen transmission. When heterozygous with normal chromosomes, a low level of recombination within the duplicated regions is detectable and the duplication and normals are recovered with equal frequencies through the female. In the pollen, the hyperploid grains cannot compete equally with the euploids in achieving fertilization.--The use of co-dominant heteromultimeric isozymes as genetic markers for the development of a series of interstitial segmental trisomics in maize is discussed.

マダイの生化学的多型に関する遺伝学的研究

Thirteen isozymes of various organs and sarcoplasmic protein of muscle of the red sea bream, Pagrus major (Temminck et Schlegel), were assayed by the horizontal starch-gel electro-phoresis in order to detect the genetic variation which would be useful as the maker in subpopulation and breeding studies. Polymorphism was found in various isozyme systems such as ADH, esterase, α-GDH, GOT, ICD, LDH, MDH, 6-PGD, PGM, PHI, and SDH. Based on the polymorphic banding pattern of each isozyme, two alleles were presumed in the respective loci, such as α-Gdh, Got-III, Icd, Ldh-B, Pgm, and Sdh, three alleles in Adh, Got-II, Mdh, 6-Pgd, and Phi-II loci, and 8 alleles in Est locus. There were no significant differences between observed proportion of phenotypes and their HARDY-WEINBERG expectation in most of the loci examined. The proportion of polymorphic loci was 34.3%, a relatively high value in comparison with other marine fishes. The proportion of occurrence of Heterozygous loci per individual was 6.6%, a comparatively similar rate to other marine fishes. The growth rate of wild red sea bream at 1 year old was independent of polymorphism in each enzyme system. It was concluded that the ADH, EST, 6-PGD, PGM, and SDH isozymes would be useful as characteristics of subpopulation and as genetic markers of the family and brother-sister in breeding studies.

Genetic analysis of alcohol dehydrogenase isozymes in pearl millet (Pennisetum typhoides).

Pearl millet (Pennisetum typhoides) produces three ADH isozymes, sets I, II, and III, with set III being expressed only in anaerobically treated seeds of seedlings. Variant strains have been identified which produce ADH isozymes with altered electrophoretic mobilities for sets I and II but not for set III activity. Based on genetic analysis of these variants and on dissociation-reassociation experiments, we propose that the three ADH isozymes are dimers of subunits coded by two structural genes, Adh1 and Adh2, with set I being a homodimer specified by Adh1, set III a homodimer specified by Adh2, and set II a heterodimer formed between the products of Adh1 and Adh2.

Isozymes of Culex pipiens quinquefasciatus (Diptera: Culicidae). II. Genetics of an alcohol dehydrogenase.

Three zones of ADH activity were observed in the mosquito Culex pipiens quinquefasciatus . Variants were found only in zone I. Genetic studies on these variants suggest that the codominant alleles Adh-l S and Adh-l F are responsible for the 3 phenotypes observed (slow band, fast band and the 3- banded pattern). The Adh-l locus is located in linkage group II. The gene order is Adh-l-y-ru . The average recombination in the Adh-l-y segment is 9.4 ± 1.01. Gene frequency studies showed that Adh-l S was the more abundant allele in all natural populations tested. Most of the laboratory populations reared for over 3 years showed fixation of this allele. ADH isozymes show relatively low substrate specificity to various alcohols tested.

Alcohol dehydrogenase polymorphism in Apis mellifera.

A polymorphic system of ADH isozymes is described in the honeybee Apis mellifera. Three and six different electrophoretic patterns were found, respectively, in drone and worker pupae analysis. The data indicate that the ADH isozymes are controlled by three alleles, Adh-1(1), Adh-1(2), and Adh-1(3). The frequency of the Adh-1 alleles is different in two analyzed subspecies, Apis mellifera adansonii (African bees) and Apis mellifera ligustica (Italian bees). In the African bees, the frequencies are 0.256 and 0.697 for Adh-1(1) and Adh-1(2), respectively. In the Italian bees, these values are shown to be 0.902 and 0.098, respectively. The allele Adh-1(3) was not detected in the Italian bee population. The effect of NAD on the resolution of this system was investigated, and only one region of ADH activity was obtained in drone pupae analysis when NAD was used in the gels. However, two different regions of activity were observed in the same samples, in the absence of the coenzyme. ADH activity was not detected in young larvae, but it increased to a maximum in prepupal and white-eyed pupal phases. It then declined progressively to total absence in the emerging bees.

Dimerization of multiple maize ADHs studied in vivo and in vitro.

Anaerobically induced primary roots simultaneously express two alcohol dehydrogenase (Adh) genes which specify three types of electrophoretically separable dimers: Set I, II, and III ADH. The S inbred line yields a particular activity ratio among these three sets. By use of an Adh1 null mutant allele and in vitro chemical dissociation and reassociation of ADH dimers, these studies extrapolate from an ADH activity ratio to the actual ratio of ADH protein. Conclusions are that (1) ADH1 and ADH2 promoters dimerize randomly in vivo and in vitro, (2) the heterodimeric isozyme (Set II) is approximately the enzymological sum of its subunits under these assay conditions, and (3) ADH-2 subunits are from 10 to 20% as active as ADH1 subunits under these assay conditions. These conclusions imply that the unlinked Adh genes are coordinately regulated and reconfirm the two-gene-three-dimer model for the maize ADH isozymes.

Simultaneous induction by anaerobiosis or 2,4-D of multiple enzymes specificed by two unlinked genes: differential Adh1-Adh2 expression in maize.

The data of this paper partially define a two-gene, differentially inducible enzyme system in maize. Four major conclusions are drawn. (1) Anaerobic treatment results in the simultaneous expression of two unlinked Adh genes, Adh1 and Adh2. Adh2 is scarcely expressed in the uninduced root and negligibly expressed in the quiescent embryo. (2) The zero-order rate of anaerobic ADH protein induction reflects the zero-order rate of ADH synthesis throughout the induction; all active ADH isozymes display negligible turnover during the induction. (3) The auxin, 2,4-D, overcomes “repression” by air. The aerobic induction rates are also zero-order with negligible turnover for any isozyme. (4) The ratio of Adh1-Adh2 expression is drastically altered dependent on the mode of induction. The level of this differential regulatory phenomenon is before or at the assembly of ADH polypeptides into enzymologically or antigenically active dimers.

Studies on the properties of the human alcohol dehydrogenase isozymes determined by the different loci ADH1, ADH2, ADH3.

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Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, ADH1, ADH2, and ADH3.

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Genetic relationships between the multiple alcohol dehydrogenases of maize.

There are three electrophoretically separable sets of alcohol dehydrogenase isozymes in maize. Previous work has shown that two of these isozymes (Sets I and II) share a subunit in common, since mutations in one of the Adh genes, Adh1, alter both isozymes. A mutation in the second Adh gene, Adh2, has now been induced and recovered. This mutant allele also alters two of the three isozymes—Sets III and II. Adh1 and Adh2 appear to segregate independently. Gel filtration data show that all ADH isozymes are indistinguishable in size. These findings support the hypothesis that the two Adh genes specify promoters which homo- and heterodimerize, yielding three types of ADH isozymes.

Alcohol dehydrogenase isozymes in adult human stomach and liver: evidence for activity of the ADH 3 locus.

Ann. Hum. Genet., Lond. (1972), 35, 243 Pyinted in Great Britain Alcohol dehydrogenase isozymes in adult human stomach and liver : evidence for activity of the ADH3 locus BY MOYRA SMITH, D. A. HOPKINSON AND HARRY HARRIS M.R.C. Human Biochemical Genetics Unit, Galton Laboratory, University College London I n a previous paper (Smith, Hopkinson & Harris, 1971) we put forward a genetical hypothesis to explain the isozyme patterns of human alcohol dehydrogenase in various tissues and at different times in development. It was suggested that there are three loci each coding for a structurally distinct type of polypeptide chain; that the isozymes are dimers; and that any particular isozyme may be made up of two identical subunits coded by a specific allele at one of the loci, or of two non-identical subunits coded by alleles at two separate loci, or of two non-identical subunits coded by different alleles at the same locus. The loci were called ADH,, ADH, and ADH, and the corresponding polypeptide subunits a, /3 and y . At each of the ADH, and ADH, loci the evidence indicated that two different common alleles occur, coding for structurally distinct forms of the corresponding polypeptide. According to the hypothesis, the isozymes in the cells of a particular tissue at a given time in development depend on the relative activities of the three loci. Thus in liver, a polypeptides determined by ADH, appear to predominate in early foetal life, but in the course of foetal develop- ment /3 polypeptides determined by ADH, appear in increasing amounts, so that while in the early foetus the main isozyme observed is aa, as development proceeds the isozymes a/3 and /3/3 appear in increasing quantities. I n adult liver ADH, activity exceeds ADH, activity. In lung, kidney and the gastro-intestinal tract the total alcohol dehydrogenase activity is very much less than in liver, and the contributions made by the different loci to the total activity show striking differences. I n lung, polypeptides determined by ADH, appear to predominate both in foetal life and in the adult. I n kidney y polypeptides determined by ADH, predominate throughout foetal life but diminish after birth, and in the adult the ADH activity that can be detected appears to be mainly derived from ADH,. I n the gastro-intestinal tract y polypeptides determined by ADH, are found as in the kidney to predominate throughout foetal life. But because of lack of suitable material the situation in adult gastro-intestinal tract was not established in our earlier work. The findings reported in the present paper are concerned with two aspects of the problem. The first concerns the ADH isozymes in the adult gastro-intestinal tract. I n our previous studies we had attempted to examine this question using material from the intestine obtained at autopsy. However, sufficiently clear and consistent isozyme patterns were not obtained. We have now found, however, that adult stomach samples from autopsy give clearly defined isozyme patterns and these correspond to those previously observed in foetal kidney and foetal intestine. Thus it appears that most of the ADH activity in adult stomach is derived from the ADH, locus. The second topic we consider here concerns certain isozymes which had previously been observed in adult liver, but which at that time could not be easily accounted for in terms of the three-locus hypothesis. These isozymes occur in addition to the aa, a/3 and /3/3 isozymes of liver, and it had been noted that they show marked variations from individual to individual in their