Abstract:
:Crs5 is a Saccharomyces cerevisiae Metallothionein (MT), non-homologous to the paradigmatic Cu-thionein Cup1. Although considered a secondary copper-resistance agent, we show here that it determines survival under zinc overload in a CUP1-null background. Its overexpression prevents the deleterious effects exhibited by CUP1-CRS5-null cells when exposed to combined Zn/Cu, as it does the mouse MT1 Zn-thionein, but not Cup1. The detailed characterization of Crs5 in vivo and in vitro Zn(II)-, Cd(II)- and Cu(I)-binding abilities fully supports its resemblance to mammalian MTs. Hence, Crs5 exhibits a good divalent metal-binding ability, yielding homometallic, highly chiral and stable Zn and Cd complexes when expressed in media enriched with these metal ions. In Cu-supplemented cultures, heterometallic Zn,Cu complexes are recovered, unless aeration is kept to a minimum. These features define a Crs5 dual metal-binding behaviour that is significantly closer to Zn-thioneins than to Cu-thioneins. Protein sequence similarities fully support these findings. Overall, a Crs5 function in global metal cell homeostasis, based on its Zn-binding features, is glimpsed. The comparative evaluation of Crs5 in the framework of MT functional differentiation and evolution allows its consideration as a representative of the primeval eukaryotic forms that progressively evolved to give rise to the Zn-thionein lineage.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Pagani A,Villarreal L,Capdevila M,Atrian Sdoi
10.1111/j.1365-2958.2006.05510.xsubject
Has Abstractpub_date
2007-01-01 00:00:00pages
256-69issue
1eissn
0950-382Xissn
1365-2958pii
MMI5510journal_volume
63pub_type
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