Literature DB >> 28565446

BIOCHEMICAL EVOLUTION ASSOCIATED WITH ANTIPREDATOR ADAPTATION IN DAMSELFLIES.

Mark A McPeek1.   

Abstract

Previous studies have shown that at least two lineages of Enallagma damselflies (Odonata: Coenagrionidae) shifted from inhabiting lakes with fish as top predators to inhabiting ponds and lakes with large dragonflies as the top predators. In adapting to living with the new predator type, these lineages evolved much greater swimming speeds to avoid attacking dragonflies. In this paper, I test whether biochemical adaptations to fuel swimming arose in concert with previously identified morphological changes that increase swimming speed. I assayed the mass-specific enzyme activities of three enzymes involved in fueling strenuous activity: pyruvate kinase and lactate dehydrogenase (enzymes involved in glycolysis) and arginine kinase (the enzyme that recharges the ATP pool). Enzyme activities were determined for 14 Enallagma species from across the genus. Species that coexist with dragonfly predators had significantly higher mass-specific arginine kinase activities than species that coexist with fish, and the results of evolutionary contrasts analyses indicate that this difference between the two groups is the result of evolutionary change associated with the habitat shifts of lineages from fish lakes to dragonfly lakes. Although significant evolution was documented for lactate dehydrogenase and pyruvate kinase across the genus, evolutionary change in the activities of these enzymes was not consistent with adaptation to coexisting with dragonfly predators. Swimming bouts to avoid dragonfly predators last for only a few seconds, and the action of arginine kinase to phosphorylate ADP to make ATP will extend the duration of maximal exertion for swimming for a few seconds. However, much longer time periods (over 45 sec) are required to generate ATP via glycolysis. Therefore, selection may have favored adaptation only at the arginine kinase locus. © 1999 The Society for the Study of Evolution.

Entities:  

Keywords:  Adaptation; Enallagma; Odonata; arginine kinase; enzyme activity; metabolism

Year:  1999        PMID: 28565446     DOI: 10.1111/j.1558-5646.1999.tb04566.x

Source DB:  PubMed          Journal:  Evolution        ISSN: 0014-3820            Impact factor:   3.694


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