Journal
FEBS LETTERS
Volume 569, Issue 1-3, Pages 289-292Publisher
WILEY
DOI: 10.1016/j.febslet.2004.06.008
Keywords
Cu,Zn superoxide dismutase; ZnuA; zinc uptake; monomer-dimer equilibrium; quaternary structure; metallochaperone
Ask authors/readers for more resources
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. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available