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Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast.

Journal article
Authors Therese Jacobson
Smriti Priya
Sandeep K Sharma
Stefanie Andersson
Sofia Jakobsson
Robbe Tanghe
Arghavan Ashouri
Sebastien Rauch
Pierre Goloubinoff
Philipp Christen
Markus J. Tamás
Published in Molecular and Cellular Biology
Volume 37
Issue 17
ISSN 1098-5549
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Language en
Subject categories Molecular biology, Toxicology, Cell and molecular biology, Biochemistry, Microbiology, Cell Biology, Biochemistry and Molecular Biology


Cadmium is a highly poisonous metal and is classified as a human carcinogen. While its toxicity is undisputed, the underlying in vivo molecular mechanisms are not fully understood. Here, we demonstrate that cadmium induces aggregation of cytosolic proteins in living Saccharomyces cerevisiae cells. Cadmium primarily targets proteins in the process of synthesis or folding, probably by interacting with exposed thiol groups in not-yet-folded proteins. On the basis of in vitro and in vivo data, we show that cadmium-aggregated proteins form seeds that increase the misfolding of other proteins. Cells that cannot efficiently protect the proteome from cadmium-induced aggregation or clear the cytosol of protein aggregates are sensitized to cadmium. Thus, protein aggregation may contribute to cadmium toxicity. This is the first report on how cadmium causes misfolding and aggregation of cytosolic proteins in vivo The proposed mechanism might explain not only the molecular basis of the toxic effects of cadmium but also the suggested role of this poisonous metal in the pathogenesis of certain protein-folding disorders.

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