Metal binding properties and structure of a type III metallothionein from the metal hyperaccumulator plant Noccaea caerulescens.
Biochim Biophys Acta
; 1824(9): 1016-23, 2012 Sep.
Article
em En
| MEDLINE
| ID: mdl-22668884
ABSTRACT
Metallothioneins (MT) are low molecular weight proteins with cysteine-rich sequences that bind heavy metals with remarkably high affinities. Plant MTs differ from animal ones by a peculiar amino acid sequence organization consisting of two short Cys-rich terminal domains (containing from 4 to 8 Cys each) linked by a Cys free region of about 30 residues. In contrast with the current knowledge on the 3D structure of animal MTs, there is a striking lack of structural data on plant MTs. We have expressed and purified a type III MT from Noccaea caerulescens (previously Thlaspi caerulescens). This protein is able to bind a variety of cations including Cd(2+), Cu(2+), Zn(2+) and Pb(2+), with different stoichiometries as shown by mass spectrometry. The protein displays a complete absence of periodic secondary structures as measured by far-UV circular dichroism, infrared spectroscopy and hydrogen/deuterium exchange kinetics. When attached onto a BIA-ATR biosensor, no significant structural change was observed upon removing the metal ions.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Metais Pesados
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Brassicaceae
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Metalotioneína
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Bélgica