Decay of Mutualistic Potential in Aphid Endosymbionts Through Silencing of Biosynthetic Loci: Buchnera of Diuraphis

Proc Biol Sci. 2000 Jul 22;267(1451):1423-31. doi: 10.1098/rspb.2000.1159.

Abstract

Buchnera, the primary bacterial endosymbiont of aphids, is known to provision essential amino acids lacking in the hosts' diet of plant sap. The recent discovery of silenced copies of genes for tryptophan biosynthesis (trpEG) in certain Buchnera lineages suggests a decay in symbiotic functions in some aphid species. However, neither the distribution of pseudogenes among lineages nor the impact of this gene silencing on amino-acid availability in hosts has been assessed. In Buchnera of the aphid Diuraphis noxia, tandem repeats of these pseudogenes have persisted in diverse lineages, and thpEG pseudogenes have originated at least twice within this aphid genus. Measures of amino-acid concentrations in Diuraphis species have shown that the presence of the pseudogene is associated with a decreased availability of tryptophan, indicating that gene silencing decreases nutrient provisioning by symbionts. In Buchnera of Diuraphis, rates of nonsynonymous substitutions are elevated in functional trpE copies, supporting the hypothesis that pseudogene origin and persistence reflect a reduced selection for symbiont biosynthetic contributions. The parallel evolution of trpEG pseudogenes in Buchnera of Diuraphis and certain other aphid hosts suggests that either selection at the host level is not effective or that fitness in these aphids is not limited by tryptophan availability.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Anthranilate Synthase*
  • Aphids / microbiology*
  • Base Sequence
  • Buchnera / genetics*
  • DNA, Bacterial
  • Gene Silencing*
  • Genes, Bacterial*
  • Molecular Sequence Data
  • Nitrogenous Group Transferases / genetics*
  • Pseudogenes
  • Sequence Homology, Nucleic Acid
  • Symbiosis*

Substances

  • DNA, Bacterial
  • Nitrogenous Group Transferases
  • Anthranilate Synthase
  • anthranilate synthase, glutamine amidotransferase subunit