ArticleJournal of molecular evolution1997
Selection and methionine accumulation in the fat body protein 2 gene (FBP2), a duplicate of the Drosophila alcohol dehydrogenase (ADH) gene.
Article in Journal of molecular evolution, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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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5 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Functional constraints of alcohol dehydrogenase (ADH) of tephritidae and relationships with other Dipteran species.Journal of molecular evolution · 2004Article
- A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Exploring the evolutionary history of the alcohol dehydrogenase gene (Adh) duplication in species of the family tephritidae.Journal of molecular evolution · 2003Article
- Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The Drosophila fat body protein 2 gene (Fbp2) is an ancient duplication of the alcohol dehydrogenase gene (Adh) which encodes a protein that differs substantially from ADH in its methionine content. In D. melanogaster, there is one methionine in ADH, while there are 51 (20% of all amino acids) in FBP2. Methionine is involved in 46% of amino acid replacements when Fbp2 DNA sequences are compared between D. melanogaster and D. pseudoobscura. Methionine accumulation does not affect conserved residues of the ADH-ADHr-FBP2 multigene family. The multigene family has evolved by replacement of mildly hydrophobic amino acids by methionine with no apparent reversion. Its short-term evolution was compared between two Drosophila species, while its long-term evolution was compared between two genera belonging respectively to acalyptrate and calyptrate Diptera, Drosophila and Sarcophaga. The pattern of nucleotide substitution was consistent with an independent accumulation of methionines at the Fbp2 locus in each lineage. Under a steady-state model, the rate of methionine accumulation was constant in the lineage leading to Drosophila, and was twice as fast as that in the calyptrate lineage. Substitution rates were consistent with a slight positive selective advantage for each methionine change in about one-half of amino acid sites in Drosophila. This shows that selection can potentially account for a large proportion of amino acid replacements in the molecular evolution of proteins.
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