67
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide-resistant insects

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Here, we compare the evolutionary routes by which bacteria and insects have evolved enzymatic processes for the degradation of four classes of synthetic chemical insecticide. For insects, the selective advantage of such degradative activities is survival on exposure to the insecticide, whereas for the bacteria the advantage is simply a matter of access to additional sources of nutrients. Nevertheless, bacteria have evolved highly efficient enzymes from a wide variety of enzyme families, whereas insects have relied upon generalist esterase-, cytochrome P450- and glutathione- S-transferase-dependent detoxification systems. Moreover, the mutant insect enzymes are less efficient kinetically and less diverged in sequence from their putative ancestors than their bacterial counterparts. This presumably reflects several advantages that bacteria have over insects in the acquisition of new enzymatic functions, such as a broad biochemical repertoire from which new functions can be evolved, large population sizes, high effective mutation rates, very short generation times and access to genetic diversity through horizontal gene transfer. Both the insect and bacterial systems support recent theory proposing that new biochemical functions often evolve from ‘promiscuous’ activities in existing enzymes, with subsequent mutations then enhancing those activities. Study of the insect enzymes will help in resistance management, while the bacterial enzymes are potential bioremediants of insecticide residues in a range of contaminated environments.

          Related collections

          Most cited references244

          • Record: found
          • Abstract: found
          • Article: found

          Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics.

          Xenobiotic resistance in insects has evolved predominantly by increasing the metabolic capability of detoxificative systems and/or reducing xenobiotic target site sensitivity. In contrast to the limited range of nucleotide changes that lead to target site insensitivity, many molecular mechanisms lead to enhancements in xenobiotic metabolism. The genomic changes that lead to amplification, overexpression, and coding sequence variation in the three major groups of genes encoding metabolic enzymes, i.e., cytochrome P450 monooxygenases (P450s), esterases, and glutathione-S-transferases (GSTs), are the focus of this review. A substantial number of the adaptive genomic changes associated with insecticide resistance that have been characterized to date are transposon mediated. Several lines of evidence suggest that P450 genes involved in insecticide resistance, and perhaps insecticide detoxification genes in general, may share an evolutionary association with genes involved in allelochemical metabolism. Differences in the selective regime imposed by allelochemicals and insecticides may account for the relative importance of regulatory or structural mutations in conferring resistance.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Rates of spontaneous mutation.

            Rates of spontaneous mutation per genome as measured in the laboratory are remarkably similar within broad groups of organisms but differ strikingly among groups. Mutation rates in RNA viruses, whose genomes contain ca. 10(4) bases, are roughly 1 per genome per replication for lytic viruses and roughly 0.1 per genome per replication for retroviruses and a retrotransposon. Mutation rates in microbes with DNA-based chromosomes are close to 1/300 per genome per replication; in this group, therefore, rates per base pair vary inversely and hugely as genome sizes vary from 6 x 10(3) to 4 x 10(7) bases or base pairs. Mutation rates in higher eukaryotes are roughly 0.1-100 per genome per sexual generation but are currently indistinguishable from 1/300 per cell division per effective genome (which excludes the fraction of the genome in which most mutations are neutral). It is now possible to specify some of the evolutionary forces that shape these diverse mutation rates.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Protein dynamism and evolvability.

              The traditional view that proteins possess absolute functional specificity and a single, fixed structure conflicts with their marked ability to adapt and evolve new functions and structures. We consider an alternative, "avant-garde view" in which proteins are conformationally dynamic and exhibit functional promiscuity. We surmise that these properties are the foundation stones of protein evolvability; they facilitate the divergence of new functions within existing folds and the evolution of entirely new folds. Packing modes of proteins also affect their evolvability, and poorly packed, disordered, and conformationally diverse proteins may exhibit high evolvability. This dynamic view of protein structure, function, and evolvability is extrapolated to describe hypothetical scenarios for the evolution of the early proteins and future research directions in the area of protein dynamism and evolution.
                Bookmark

                Author and article information

                Journal
                Evol Appl
                Evol Appl
                eva
                Evolutionary Applications
                Blackwell Publishing Ltd (Oxford, UK )
                1752-4571
                1752-4571
                March 2011
                : 4
                : 2
                : 225-248
                Affiliations
                simpleCSIRO Ecosystem Sciences Canberra, ACT, Australia
                Author notes
                John G. Oakeshott, CSIRO Ecosystem Sciences, GPO Box 1700, Clunies Ross Street, Canberra, ACT 2601, Australia. Tel.: +61 2 6246 4157; fax: +61 2 6246 4094; e-mail: john.oakeshott@ 123456csiro.au
                [*]

                Current address: Research School of Chemistry, The Australian National University, Canberra, ACT 2601, Australia.

                Article
                10.1111/j.1752-4571.2010.00175.x
                3352558
                25567970
                8955ceef-3405-434a-b30d-bb2401eba1e3
                © 2011 CSIRO
                History
                : 25 October 2010
                : 12 November 2010
                Categories
                Original Article

                Evolutionary Biology
                pyrethroids,carbamates,organochlorines,hydrolases,organophosphates
                Evolutionary Biology
                pyrethroids, carbamates, organochlorines, hydrolases, organophosphates

                Comments

                Comment on this article

                scite_

                Similar content153

                Cited by27

                Most referenced authors1,857