Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Berducci G,Mazzetti AP,Rotilio G,Battistoni Adoi
10.1016/j.febslet.2004.06.008keywords:
subject
Has Abstractpub_date
2004-07-02 00:00:00pages
289-92issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304007252journal_volume
569pub_type
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