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Periplasmic competition for zinc uptake between the metallochaperone ZnuA and Cu,Zn superoxide dismutase
Author(s) -
Berducci Giovanni,
Mazzetti Anna Paola,
Rotilio Giuseppe,
Battistoni Andrea
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.008
Subject(s) - periplasmic space , zinc , biochemistry , escherichia coli , chemistry , superoxide dismutase , cytoplasm , mutant , dismutase , bacteria , osmolyte , enzyme , biology , genetics , organic chemistry , gene
We have investigated the availability of zinc in the periplasmic space of Escherichia coli using a mutant Cu,Zn superoxide dismutase whose dimerization is triggered by zinc binding. This mutant enzyme accumulates in the monomeric form when wild type cells are grown in minimal medium, but assembles in the dimeric form when it is produced in the same medium by a mutant strain lacking the periplasmic zinc metallochaperone ZnuA. These results indicate that periplasmic zinc‐containing proteins compete for metal binding when bacteria grow in environments where this element is present in traces. The effective ZnuA ability to sequester the available zinc ions from the periplasm suggests that zinc‐containing cytoplasmic proteins are more important for bacterial viability than the periplasmic ones.