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Int. J. Mol. Sci. 2016, 17(1), 6; doi:10.3390/ijms17010006

Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein?

1
Departament de Química, Facultat de Ciències, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
2
Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Av. Diagonal 643, E-08028 Barcelona, Spain
3
Institute of Organic Chemistry, University of Zurich, 8057 Zurich, Switzerland
4
Institute of Zoology, University of Innsbruck, Technikerstraße 25, A-6020 Innsbruck, Austria
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Nick Hadjiliadis
Received: 17 November 2015 / Revised: 11 December 2015 / Accepted: 14 December 2015 / Published: 22 December 2015
(This article belongs to the Special Issue Metal Metabolism in Animals)
View Full-Text   |   Download PDF [1285 KB, uploaded 23 December 2015]   |  

Abstract

Snail metallothioneins (MTs) constitute an ideal model to study structure/function relationships in these metal-binding polypeptides. Helix pomatia harbours three MT isoforms: the highly specific CdMT and CuMT, and an unspecific Cd/CuMT, which represent paralogous proteins with extremely different metal binding preferences while sharing high sequence similarity. Preceding work allowed assessing that, although, the Cys residues are responsible for metal ion coordination, metal specificity or preference is achieved by diversification of the amino acids interspersed between them. The metal-specific MT polypeptides fold into unique, energetically-optimized complexes of defined metal content, when binding their cognate metal ions, while they produce a mixture of complexes, none of them representing a clear energy minimum, with non-cognate metal ions. Another critical, and so far mostly unexplored, region is the stretch linking the individual MT domains, each of which represents an independent metal cluster. In this work, we have designed and analyzed two HpCdMT constructs with substituted linker segments, and determined their coordination behavior when exposed to both cognate and non-cognate metal ions. Results unequivocally show that neither length nor composition of the inter-domain linker alter the features of the Zn(II)- and Cd(II)-complexes, but surprisingly that they influence their ability to bind Cu(I), the non-cognate metal ion. View Full-Text
Keywords: Cd-isoform; domain linker sequence; Helix pomatia; metallothionein; metal binding Cd-isoform; domain linker sequence; Helix pomatia; metallothionein; metal binding
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Gil-Moreno, S.; Jiménez-Martí, E.; Palacios, Ò.; Zerbe, O.; Dallinger, R.; Capdevila, M.; Atrian, S. Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein? Int. J. Mol. Sci. 2016, 17, 6.

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