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Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity
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Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity
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Journal Article
Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity
2016
Overview
Bacteria are thought to avoid using the essential metal ion copper in their cytosol due to its toxicity. Herein we characterize Csp3, the cytosolic member of a new family of bacterial copper storage proteins from
Methylosinus trichosporium
OB3b and
Bacillus subtilis
. These tetrameric proteins possess a large number of Cys residues that point into the cores of their four-helix bundle monomers. The Csp3 tetramers can bind a maximum of approximately 80 Cu(I) ions, mainly via thiolate groups, with average affinities in the (1–2) × 10
17
M
−1
range. Cu(I) removal from these Csp3s by higher affinity potential physiological partners and small-molecule ligands is very slow, which is unexpected for a metal-storage protein.
In vivo
data demonstrate that Csp3s prevent toxicity caused by the presence of excess copper. Furthermore, bacteria expressing Csp3 accumulate copper and are able to safely maintain large quantities of this metal ion in their cytosol. This suggests a requirement for storing copper in this compartment of Csp3-producing bacteria.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Bacillus subtilis - drug effects
/ Bacillus subtilis - metabolism
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Copper
/ Cytosol
/ Humanities and Social Sciences
/ Ions
/ Methylosinus trichosporium - drug effects
/ Methylosinus trichosporium - metabolism
/ Monomers
/ Protective Agents - chemistry
/ Protective Agents - metabolism
/ Protein Structure, Secondary
/ Proteins
/ Science
/ Toxicity
