Shaping mechanisms of metal specificity in a family of metazoan metallothioneins: evolutionary differentiation of mollusc metallothioneins |
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Authors: | Òscar Palacios Ayelen Pagani Sílvia Pérez-Rafael Margit Egg Martina Höckner Anita Brandstätter Mercè Capdevila Sílvia Atrian Reinhard Dallinger |
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Institution: | 1.Departamento Química, Faculty Ciències,Universitat Autònoma de Barcelona, Cerdanyola del Vallès,Barcelona,Spain;2.Departamento Genètica, Faculty Biologia,Universitat de Barcelona,Barcelona,Spain;3.Institute of Zoology and Center of Molecular Biosciences Innsbruck (CMBI),University of Innsbruck,Innsbruck,Austria;4.Division of Genetic Epidemiology, Department of Medical Genetics, Molecular and Clinical Pharmacology,Innsbruck Medical University,Austria |
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Abstract: | Background The degree of metal binding specificity in metalloproteins such as metallothioneins (MTs) can be crucial for their functional
accuracy. Unlike most other animal species, pulmonate molluscs possess homometallic MT isoforms loaded with Cu+ or Cd2+. They have, so far, been obtained as native metal-MT complexes from snail tissues, where they are involved in the metabolism
of the metal ion species bound to the respective isoform. However, it has not as yet been discerned if their specific metal
occupation is the result of a rigid control of metal availability, or isoform expression programming in the hosting tissues
or of structural differences of the respective peptides determining the coordinative options for the different metal ions.
In this study, the Roman snail (Helix pomatia) Cu-loaded and Cd-loaded isoforms (HpCuMT and HpCdMT) were used as model molecules in order to elucidate the biochemical
and evolutionary mechanisms permitting pulmonate MTs to achieve specificity for their cognate metal ion. |
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