Insertion of the retroposable element, jockey, near the Adh gene of Drosophila melanogaster is associated with altered gene expression (original) (raw)
Related papers
Characterization of the Adh(sl) Regulatory Mutation in Drosophila Melanogaster
Genetics, 1988
We describe the characterization of a previously reported control mutation, Adh(SL), in the alcohol dehydrogenase gene of Drosophila melanogaster, which results in decreased production of ADH molecules and subsequently lower ADH activity in adults. We find that the regulatory element modifies ADH mRNA levels and acts cis on both ADH protein and mRNA. It is not promoter specific but is developmentally specific to the adult stage. The Adh(SL) allele carries a 4.5-kb insert approximately 3 kb 5' to the distal promoter. This new insertion may be responsible for the regulatory phenotype of Adh(SL).
Genetics, 2010
Although most amino acids can be encoded by more than one codon, the synonymous codons are not used with equal frequency. This phenomenon is known as codon bias and appears to be a universal feature of genomes. The translational selection hypothesis posits that the use of optimal codons, which match the most abundant species of isoaccepting tRNAs, results in increased translational efficiency and accuracy. Previous work demonstrated that the experimental reduction of codon bias in the Drosophila alcohol dehydrogenase (Adh) gene led to a significant decrease in ADH protein expression. In this study we performed the converse experiment: we replaced seven suboptimal leucine codons that occur naturally in the Drosophila melanogaster Adh gene with the optimal codon. We then compared the in vivo ADH activities imparted by the wild-type and mutant alleles. The introduction of optimal leucine codons led to an increase in ADH activity in third-instar larvae. In adult flies, however, the introduction of optimal codons led to a decrease in ADH activity. There is no evidence that other selectively constrained features of the Adh gene, or its rate of transcription, were altered by the synonymous replacements. These results are consistent with translational selection for codon bias being stronger in the larval stage and suggest that there may be a selective conflict over optimal codon usage between different developmental stages.
Two alternate transcripts of the single copy Alcohol dehydrogenase (Adh) gene accumulate with developmental specificity in all of 12 species of Hawaiian picturewinged Drosophila which have been examined. Relative to the paradigm species D. affinidisjuncta, the Adh transcript normally restricted to larvae is found to accumulate in both larval and adult tissues in D. formella. T h e other Adh transcript, which normally accumulates only in adults, accumulates in third-instar D. prostopalpis larvae as well. In species hybrids, the D. formella phenotype shows additive inheritance. These observations document the existence of a novel type of genetic variability. Furthermore, such variants suggest specific properties for the biological systems that regulate ADH expression in Drosophila, and they should facilitate further experimental investigations.
Proceedings of the National Academy of Sciences, 1990
Drosophila melanogaster and its sibling species, Drosophila simulans, differ in expression of the enzyme alcohol dehydrogenase (ADH). Adult melanogaster flies that are homozygous for the Slow allozyme have approximately twice the level of ADH activity and crossreacting material as simulans adults. There is no corresponding difference in ADH mRNA, however, so this difference in ADH protein level is evidently due to a difference in the rate of translation of the two RNAs and/or to a difference in protein stability. Here we report an interspecific gene-transfer experiment, using P-element transformation, to determine whether this expression difference is due to genetic background differences between the species (trans-acting modifiers) or to cis-acting factors within the Adh gene. When the Adh genes from D. melanogaster and D. simulans are put into the same genetic background, there is no detectable difference in their level of expression. The level is relatively high in the melanogaster background and relatively low in the simulans background. Therefore, the interspecific difference in Adh expression is due entirely to trans-acting modifiers, in spite of the many sequence differences between the Adh genes of the two species, which include two amino acid substitutions.
Cryptic variants at the Adh locus in drosophila melanogaster
Cryptic variants at the Adh locus in drosophila melanogaster, 2018
Fifty-two specially constructed isochromosomal lines from 16 Mexican strains of D. melanogaster were employed to ascertain the extent of genetic variation of alcohol dehydrogenase (ADH) activity between and within the populations, and to investigate the regulatory mechanisms which operate to control enzyme activity levels during development. Native ADH activity for each line was assayed spectrophotometrically. Variation in ADH activity was demonstrated among and within the populations. The native ADH activity levels of the lines when compared to those after treatment with guanidine hydrochloride, urea and heat revealed that while some lines for the AdhI or AdhII allele were highly susceptible to these denaturants others showed a high degree of resistance. These observations clearly indicated that cryptic variation at a biochemical level does exist among and within the populations of D. melanogaster. Significant correlations were noted between the native ADH activity and the enzyme activity after treatment. The cryptic variant lines exhibited modifications in terms of their susceptibility/ resistance properties during different developmental stages under variable temperatures. The results strongly suggested that the increased biochemical variation of ADH activity has adaptive significance for the individual during development.
Differential regulation of duplicate alcohol dehydrogenase genes in Drosophila mojavensis
Developmental Biology, 1983
These studies report the existence of multiple forms of alcohol dehydrogenase in extracts of Droso&ilu mojaoensis. The existence of these forms can be best explained by the hypothesis of a duplication for the Adh locus in D. mojnr,ensis. Electrophoretic variants at each locus have been identified and crosses between individuals carrying alternative alleles at each locus result in F1 progeny with six bands of ADH. This pattern is consistent with these individuals being heterozygous at two loci. The loci have been named Adh-1 and Adh-2. Examination of the isozyme content during development shows that the two Adh genes are not coordinately controlled but have separate developmental programs. In embryos and first and second instar larvae only Adh-I is expressed. At about the time of the second molt Adh-2 expression commences in some of the same cells that previously expressed and continue to express Adh-1. This is evidenced by the existence of an interlocus heterodimer in third instar larvae. Both genes are expressed throughout pupation. Shortly after emergence Adh-I expression declines. In mature males only ADH-2 is present. In mature females both Adh-1 and Adh-2 are expressed but not in the same cells since the interlocus heterodimer is absent, Examination of specific tissues reveals that most of the larval ADH is found in fat body cells and as in most tissues of third instar larvae both Adh-1 and Adh-2 are expressed. The single exception appears to be larval gut which contains ADH-1 but little if any ADH-2. In mature males and female flies all ADH containing tissues have only ADH-2. However, mature ovaries contain substantial quantities of ADH-1 which is apparently deposited into eggs. Given the extensive amount of available information on the Adh gene-enzyme system of D. melanogaster and the tools that can be applied to the analysis of homologous systems, the ADH duplication of D. nlojauensis and its regulation may be a useful one for studying differential gene regulation in specific cell types.
Genetica, 1991
The tissue specific patterns for Drosophila melanogaster alcohol dehydrogenase (Adh) mRNA and protein expression were determined using in situ hybridization and immunocytochemical techniques. Alcohol dehydrogenase mRNAs were localized in thin sections of frozen tissue using the hybridization of single stranded RNA probes. Alcohol dehydrogenase protein was identified in frozen tissue samples using ADH antisera, a biotinylated secondary antibody, and streptavidin conjugated to horseradish peroxidase. In tissues such as fat body, gastric caeca, and adult cardiac valve, the patterns of expression for ADH protein and mRNA were identical. Other tissues such as oocytes, nurse cells, imaginal disks, and brain show levels ofAdh mRNA that are lower than or equivalent to those observed in the previously mentioned tissues, but they exhibit little or no ADH protein. The lack of concordance between Adh mRNA and ADH protein expression in oocytes and nurse cells may reflect the packaging of maternal mRNAs (but not ADH protein) for use in early development. The reason(s) for the other discrepancies in protein and mRNA expression are not known at this time but may be due to post-transcriptional regulation in these specific tissues.
Biochemical differences between products of the Adh locus in Drosophila
1980
ABSTRACT An analysis of the molecular properties of the major alcohol dehydrogenase (EC 1.1. 1.1) allozyme variants found segregating in natural populations of D. melanogaster is presented. Our results indicate:(1) ADH-S enzyme has generally lower Michaelis-Menten constants than those of ADH-F;(2) ADH-S and ADH-F enzymes display opposite interactions for both co-factor and substrate; and (3) higher levels of ADH are associated with the Adh-fast genotype. The possible adaptive significance of these findings is discussed.
1992
Southern analysis of the Adh region of 2 12 Drosophila melanogaster lines collected from the Tahbilk winery revealed linkage disequilibrium between a 37-bp insertion [designated V2 by ] and the fast electrophoretic variant of alcohol dehydrogenase ( ADH-F) . Among these lines 34% contained the insert and encoded ADH-F, 33.5% encoded ADH-F and did not have the insert, and 32.5% encoded the slow electrophoretic variant of alcohol dehydrogenase ( ADH-S ) . Strong linkage association between this insert and ADH-F is evident worldwide. Twenty-nine of the second chromosome lines were characterized for ADH protein quantity by using radial immunodiffusion.