Copper delivery to an endospore coat protein of Bacillus subtilis

Copper delivery to an endospore coat protein of Bacillus subtilis

Blog Article

A family of cytosolic copper (Cu) storage proteins (the Csps) bind large quantities of Cu(I) via their Cys-lined four-helix bundles, and the majority are cytosolic (Csp3s).The presence of Csp3s in many bacteria appears inconsistent with the current dogma that bacteria, unlike eukaryotes, 6-0 igora vibrance have evolved not to maintain intracellular pools of Cu due to its potential toxicity.Sporulation in Bacillus subtilis has been used to investigate if a Csp3 binds Cu(I) in the cytosol for a target enzyme.

The activity of the Cu-requiring endospore here multi-Cu oxidase BsCotA (a laccase) increases under Cu-replete conditions in wild type B.subtilis.In the strain lacking BsCsp3 lower BsCotA activity is observed and is unaffected by Cu levels.

BsCsp3 loaded with Cu(I) readily activates apo-BsCotA in vitro.Experiments with a high affinity Cu(I) chelator demonstrate that Cu(I) transfer from Cu(I)-BsCsp3 must occur via an associative mechanism.BsCsp3 and BsCotA are both upregulated during late sporulation.

We hypothesise that BsCsp3 acquires cuprous ions in the cytosol of B.subtilis for BsCotA.