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Toward a property/function relationship for metallothioneins: Histidine coordination and unusual cluster composition in a zinc-metallothionein from plants

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Leszczyszyn, Oksana I., Schmid, Ralf and Blindauer, Claudia A.. (2007) Toward a property/function relationship for metallothioneins: Histidine coordination and unusual cluster composition in a zinc-metallothionein from plants. Proteins, Vol.68 (No.4). pp. 922-935. ISSN 0887-3585

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Official URL: http://dx.doi.org/10.1002/prot.21463

Abstract

Early cysteine labeled (E-c) proteins are plant metallothioneins, which were first identified in wheat embryos and are thought to be seed-specific. An exhaustive analysis of expressed sequence tag (EST) entries reveals that homologs are expressed in embryos of both classes of flowering plants (monocotyledons and dicotyledons), but also occur in conifers (gymnosperms) and seed-free spike moss (lycophyta). Mass spectrometric and elemental analysis results indicate that, contrary to the widely propagated number of five, Ec binds predominantly six zinc ions in at least two zinc-thiolate clusters. H-1 and Cd-111 NMR experiments suggest that, in contrast to the majority of previously characterized metallothioneins, two conserved histidine residues participate in metal binding. The collected data is con- sistent with the presence of clusters unprecedented in metallothioneins so far. This novel cluster composition is accompanied by metalbinding properties that are substantially different from other metallothioneins; thus wheat EC binds zinc less strongly than either mammalian or cyanobacterial MTs. The unique biochemical properties of wheat Ec render it ideally suited for a role in zinc donation to nascent proteins during seed development, a role that has been suggested based on the fact that EC is induced by the plant hormone abscisic acid, but not by heavy metals. Our results provide a step further toward developing a property/function relationship for metallothioneins.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Chemistry
Journal or Publication Title: Proteins
Publisher: John Wiley & Sons, Inc.
ISSN: 0887-3585
Date: September 2007
Volume: Vol.68
Number: No.4
Number of Pages: 14
Page Range: pp. 922-935
Identification Number: 10.1002/prot.21463
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
URI: http://wrap.warwick.ac.uk/id/eprint/31542

Data sourced from Thomson Reuters' Web of Knowledge

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