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Title: Interactions of Chaperonin with a Weakly Active Anthranilate Synthase from the Aphid Endosymbiont Buchnera Aphidicola
Authors: Huang, C. Y.;C. Y. Lee;H. C. Wu;M. H. Kuo;C. Y. Lai
Contributors: 生物系
Date: 2008-11
Issue Date: 2011-05-16T07:39:49Z
Publisher: Springer Verlag
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.
Relation: Microbial Ecology, 56(4):696-703
Appears in Collections:[生物技術研究所] 期刊論文

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