A de novo evolved domain improves the cadmium detoxification capacity of limpet metallothioneins.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
01 06 2023
01 06 2023
Historique:
received:
23
03
2023
accepted:
23
05
2023
medline:
5
6
2023
pubmed:
2
6
2023
entrez:
1
6
2023
Statut:
epublish
Résumé
Metallothioneins (MTs) constitute an important family of metal binding proteins. Mollusk MTs, in particular, have been used as model systems to better understand the evolution of their metal binding features and functional adaptation. In the present study two recombinantly produced MTs, LgiMT1 and LgiMT2, and their de novo evolved γ domain, of the marine limpet Lottia gigantea, were analyzed by electronic spectroscopy and mass spectrometry. Both MT proteins, as well as their γ domains, exhibit a strong binding specificity for Cd(II), but not for Zn(II) or Cu(I). The LgiMTs' γ domain renders an M
Identifiants
pubmed: 37264073
doi: 10.1038/s41598-023-35786-1
pii: 10.1038/s41598-023-35786-1
pmc: PMC10235030
doi:
Substances chimiques
Cadmium
00BH33GNGH
Zinc
J41CSQ7QDS
Metals
0
Metallothionein
9038-94-2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8895Informations de copyright
© 2023. The Author(s).
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