Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?

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 m...

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Autores: Gil-Moreno,Selene, Jiménez Martí, Elena, Palacios Bonilla, Òscar, Zerbe, Oliver, Dallinger, Reinhard, Capdevila, Mercè, Atrian i Ventura, Sílvia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/151817
Acceso en línea:https://hdl.handle.net/2445/151817
Access Level:acceso abierto
Palabra clave:Aliatges lleugers
Pèptids
Ions metàl·lics
Light metal alloys
Peptides
Metal ions
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spelling Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?Gil-Moreno,SeleneJiménez Martí, ElenaPalacios Bonilla, ÒscarZerbe, OliverDallinger, ReinhardCapdevila, MercèAtrian i Ventura, SílviaAliatges lleugersPèptidsIons metàl·licsLight metal alloysPeptidesMetal ionsSnail 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.MDPI2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/151817Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3390/ijms17010006International Journal of Molecular Sciences, 2015, vol. 17, num. 1, p. 6https://doi.org/10.3390/ijms17010006cc-by (c) Gil-Moreno,Selene et al., 2015http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1518172026-05-27T06:46:51Z
dc.title.none.fl_str_mv Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
title Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
spellingShingle Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
Gil-Moreno,Selene
Aliatges lleugers
Pèptids
Ions metàl·lics
Light metal alloys
Peptides
Metal ions
title_short Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
title_full Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
title_fullStr Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
title_full_unstemmed Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
title_sort Does variation of the inter-domain linker sequence modulate the metal-binding behavior of Helix pomatia Cd-metallothionein?
dc.creator.none.fl_str_mv Gil-Moreno,Selene
Jiménez Martí, Elena
Palacios Bonilla, Òscar
Zerbe, Oliver
Dallinger, Reinhard
Capdevila, Mercè
Atrian i Ventura, Sílvia
author Gil-Moreno,Selene
author_facet Gil-Moreno,Selene
Jiménez Martí, Elena
Palacios Bonilla, Òscar
Zerbe, Oliver
Dallinger, Reinhard
Capdevila, Mercè
Atrian i Ventura, Sílvia
author_role author
author2 Jiménez Martí, Elena
Palacios Bonilla, Òscar
Zerbe, Oliver
Dallinger, Reinhard
Capdevila, Mercè
Atrian i Ventura, Sílvia
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Aliatges lleugers
Pèptids
Ions metàl·lics
Light metal alloys
Peptides
Metal ions
topic Aliatges lleugers
Pèptids
Ions metàl·lics
Light metal alloys
Peptides
Metal ions
description 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.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/151817
url https://hdl.handle.net/2445/151817
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/ijms17010006
International Journal of Molecular Sciences, 2015, vol. 17, num. 1, p. 6
https://doi.org/10.3390/ijms17010006
dc.rights.none.fl_str_mv cc-by (c) Gil-Moreno,Selene et al., 2015
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Gil-Moreno,Selene et al., 2015
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Genètica, Microbiologia i Estadística)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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