Pan X~Boeke JD, 2010

Pubmed ID 20660648
Title Trivalent arsenic inhibits the functions of chaperonin complex.
Authors Xuewen Pan, Stefanie Reissman, Nick R Douglas, Zhiwei Huang, Daniel S Yuan, Xiaoling Wang, J Michael McCaffery, Judith Frydman, Jef D Boeke
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 postsynthesis. Consistent with this hypothesis, we found that arsenic treatment distorted morphology of both actin and microtubule 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.
Citation Genetics 2010; 186:725-34


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Papers Phenotype Conditions Collection Tested mutants Data Details
Pan X~Boeke JD, 2010 growth (relative abundance in pooled culture) sodium arsenite [450 mM] het ~5,996 Discrete

Curation history

Aug. 7, 2013 Data requested.
Aug. 7, 2013 Data abandoned.
Aug. 7, 2013 Tested strains requested.
Aug. 7, 2013 Tested strains abandoned.
Nov. 10, 2014 Data to load.
Sept. 26, 2016 Data loaded.