Experimental recombining of repetitive motifs leads to large functional metallothioneins and demonstrates their modular evolvability potential.

ABSTRACT: Protein modularity is acknowledged for promoting the emergence of new protein variants via domain rearrangements. Metallothioneins (MTs) offer an excellent model system for experimentally examining the consequences of domain rearrangements due to the possibility to assess the functional properties of native and artificially created variants using spectroscopic methods and metal tolerance assays. In this study, we have investigated the functional properties of AbiMT4 from the snail Alinda biplicata (Gastropoda, Mollusca), a large MT comprising 10 putative β domains (β3₉β1), alongside four artificially designed variants differing in domain number, type, or order. Our findings reveal that AbiMT4 is a cadmium-selective protein with a high metal-binding capacity, characterized by str

SUBMITTER: Dallinger R 

PROVIDER: S-EPMC11645667 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature