Copper induces significant protein aggregation under anaerobic conditions in vivo.
Cu+ ions act as efficient protein aggregating reagents in a ROS-independent manner in vitro.
Cu+ ions inactivate and unfold purified proteins in a concentration-dependent manner.
Identification and comparative analysis of copper-induced protein aggregates.
Copper induces expression of stress response genes.
Molecular chaperones protect E. coli against Cu stress.
Both copper redox states cause protein aggregation in vitro.
Gradual impact of copper on cells.
Anaerobic copper stress boosts intracellular copper levels.
Different mechanisms are involved in copper-mediated cell death.
Cellular protection against copper stress by molecular chaperones.
MATERIALS AND METHODS
Bacterial strains and culture conditions.
Cell survival after short-term exposure to copper.
Survival test after long-term exposure to copper.
Cu quantification by ICP-OES.
Purification of protein aggregates from whole cells.
Purification of protein aggregates from cell lysate.
Metal-induced protein aggregation assays.
Citrate synthase activity assay.
Sample preparation for mass spectrometry.
Data analysis and statistics for mass spectrometry.
Quantitative real-time RT-PCR.
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