ArticleGenetics2000
Deletion of a conserved regulatory element in the Drosophila Adh gene leads to increased alcohol dehydrogenase activity but also delays development.
Article in Genetics, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
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- A novel suppressive effect of alcohol dehydrogenase 5 in neuronal differentiation.The Journal of biological chemistry · 2014Article
- Transcriptome analysis in tardigrade species reveals specific molecular pathways for stress adaptations.Bioinformatics and biology insights · 2012Article
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- Pistil-function breakdown in a new S-allele of European pear, S21*, confers self-compatibility.Plant cell reports · 2009Article
- In silico investigations on functional and haplotype tag SNPs associated with congenital long QT syndromes (LQTSs).Genomic medicine · 2008Article
- Patterns of amino acid evolution in the Drosophila ananassae chimeric gene, siren, parallel those of other Adh-derived chimeras.Genetics · 2008Article
- Parallel evolution of chimeric fusion genes.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Functional analysis of Drosophila melanogaster gene regulatory sequences by transgene coplacement.Genetics · 2004Article
- Pleiotropic effect of disrupting a conserved sequence involved in a long-range compensatory interaction in the Drosophila Adh gene.Genetics · 2004Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In vivo levels of enzymatic activity may be increased through either structural or regulatory changes. Here we use Drosophila melanogaster alcohol dehydrogenase (ADH) in an experimental test for selective differences between these two mechanisms. The well-known ADH-Slow (S)/Fast (F) amino acid replacement leads to a twofold increase in activity by increasing the catalytic efficiency of the enzyme. Disruption of a highly conserved, negative regulatory element in the Adh 3' UTR also leads to a twofold increase in activity, although this is achieved by increasing in vivo Adh mRNA and protein concentrations. These two changes appear to be under different types of selection, with positive selection favoring the amino acid replacement and purifying selection maintaining the 3' UTR sequence. Using transgenic experiments we show that deletion of the conserved 3' UTR element increases adult and larval Adh expression in both the ADH-F and ADH-S genetic backgrounds. However, the 3' UTR deletion also leads to a significant increase in developmental time in both backgrounds. ADH allozyme type has no detectable effect on development. These results demonstrate a negative fitness effect associated with Adh overexpression. This provides a mechanism whereby natural selection can discriminate between alternative pathways of increasing enzymatic activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.