Reference: Pan X, et al. (2010) Trivalent arsenic inhibits the functions of chaperonin complex. Genetics 186(2):725-34

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Abstract

The exact molecular mechanisms by which the environmental pollutant arsenic works in biological systems are not completely understood. Using an unbiased chemogenomics approach in Saccharomyces cerevisiae, we found that mutants of the chaperonin complex TRiC and the functionally related prefoldin complex are all hypersensitive to arsenic compared to a wild-type strain. In contrast, mutants with impaired ribosome functions were highly arsenic-resistant. These observations led us to hypothesize that arsenic might inhibit TRiC function, required for folding of actin, tubulin, and other proteins post-synthesis. Consistent with this hypothesis, we found that arsenic-treatment distorted morphology of both actin and microtubules filaments. Moreover, arsenic impaired substrate folding by both bovine and Archaeal TRiC complexes in vitro. These results together indicate that TRiC is a conserved target of arsenic inhibition in various biological systems.

Reference Type
Journal Article
Authors
Pan X, Reissman S, Douglas NR, Huang Z, Yuan DS, Wang X, McCaffery JM, Frydman J, Boeke JD
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