Interactions of chaperonin with a weakly active anthranilate synthase from the aphid endosymbiont Buchnera aphidicola

Chia Ying Huang, Chi-Ying Lee, Hsiao Chen Wu, Mei Hwa Kuo, Chi-Yung Lai

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The endosymbiotic bacterium Buchnera provides its aphid host with essential amino acids. Buchnera is typical of intracellular symbiotic and parasitic microorganisms in having a small effective population size, which is believed to accelerate genetic drift and reduce the stability of gene products. It is hypothesized that Buchnera mitigates protein instability with an increased production of the chaperonins GroESL. In this paper, we report the expression and functional analysis of trpE, a plasmid-borne fast-evolving gene encoding the tryptophan biosynthesis enzyme anthranilate synthase. We overcame the problem of low enzyme stability by using an anthranilate synthase-deficient mutant of E. coli as the expression host and the method of genetic complementation for detection of the enzyme activity. We showed that the Buchnera anthranilate synthase was only weakly active at the temperature of 26°C but became inactive at the higher temperatures of 32°C and 37°C and that the coexpression with chaperonin genes groESL of E. coli enhanced the function of the Buchnera enzyme. These findings are consistent with the proposed role of groESL in the Buchnera-aphid symbiosis.

Original languageEnglish
Pages (from-to)696-703
Number of pages8
JournalMicrobial Ecology
Volume56
Issue number4
DOIs
Publication statusPublished - 2008 Nov 1

Fingerprint

Buchnera (Proteobacteria)
Buchnera aphidicola
anthranilate synthase
chaperonins
endosymbiont
endosymbionts
aphid
Aphidoidea
enzyme
gene
effective population size
genetic drift
symbiosis
plasmid
enzyme activity
amino acid
microorganism
genetic complementation
Escherichia coli
enzyme stability

All Science Journal Classification (ASJC) codes

  • Ecology, Evolution, Behavior and Systematics
  • Ecology
  • Soil Science

Cite this

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title = "Interactions of chaperonin with a weakly active anthranilate synthase from the aphid endosymbiont Buchnera aphidicola",
abstract = "The endosymbiotic bacterium Buchnera provides its aphid host with essential amino acids. Buchnera is typical of intracellular symbiotic and parasitic microorganisms in having a small effective population size, which is believed to accelerate genetic drift and reduce the stability of gene products. It is hypothesized that Buchnera mitigates protein instability with an increased production of the chaperonins GroESL. In this paper, we report the expression and functional analysis of trpE, a plasmid-borne fast-evolving gene encoding the tryptophan biosynthesis enzyme anthranilate synthase. We overcame the problem of low enzyme stability by using an anthranilate synthase-deficient mutant of E. coli as the expression host and the method of genetic complementation for detection of the enzyme activity. We showed that the Buchnera anthranilate synthase was only weakly active at the temperature of 26°C but became inactive at the higher temperatures of 32°C and 37°C and that the coexpression with chaperonin genes groESL of E. coli enhanced the function of the Buchnera enzyme. These findings are consistent with the proposed role of groESL in the Buchnera-aphid symbiosis.",
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Interactions of chaperonin with a weakly active anthranilate synthase from the aphid endosymbiont Buchnera aphidicola. / Huang, Chia Ying; Lee, Chi-Ying; Wu, Hsiao Chen; Kuo, Mei Hwa; Lai, Chi-Yung.

In: Microbial Ecology, Vol. 56, No. 4, 01.11.2008, p. 696-703.

Research output: Contribution to journalArticle

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