A multi-domain snail metallothionein increases cadmium resistance and fitness in Caenorhabditis elegans.

ABSTRACT: Metallothioneins (MTs) are a family of mostly low-molecular weight, cysteine-rich proteins capable of specific metal-ion binding that are involved in metal detoxification and homeostasis, as well as in stress response. In contrast to most other animal species which possess two-domain (bidominial) MTs, some gastropod species have evolved Cd²⁺-selective multidomain MTs (md-MTs) consisting of several concatenated β3 domains and a single C-terminal β1 domain. Each domain contains three-metal ion clusters and binds three metal ions. The terrestrial snail Alinda biplicata possesses, among other MT isoforms, an md-MT with nine β3 domains and a C-terminal β1 domain (termed 10md-MT), capable of binding up to 30 Cd²⁺ ions per protein molecule. In the present study, the Alinda b

SUBMITTER: Andric A 

PROVIDER: S-EPMC11513058 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature