RecARAD51

RecARAD51 is a synthetic recombinase proposed in discussions of cross-domain homologous recombination, conceived by fusing motifs from bacterial RecA with the core of eukaryotic RAD51. The aim is to leverage RecA’s robust ATPase activity and RAD51’s eukaryotic-style filament dynamics to enhance strand exchange across prokaryotic and eukaryotic systems. As a conceptual protein, RecARAD51 is typically described as a single polypeptide that combines an N-terminal RecA-like ATPase domain with a C-terminal RAD51-like DNA-binding core, connected by a flexible linker. The precise boundaries vary among designs, but both domains retain key catalytic and DNA-binding motifs.

In function, RecARAD51 is expected to form nucleoprotein filaments on single-stranded DNA and catalyze homologous pairing and strand displacement, promoting strand exchange. In theory, it could operate in a broader range of cellular environments than native Rad51 alone, though its activity would likely depend on the presence of mediator and accessory factors appropriate to each organism. In prokaryotic cells it might not require nucleus-targeting signals, while in eukaryotic cells an explicit nuclear localization signal would be needed.

Applications of the concept include testing cross-domain recombination, improving gene-targeting strategies in synthetic biology, and exploring the minimal requirements for filament-based recombination. The status of RecARAD51 remains largely experimental and theoretical, with interest focused on protein design, structural compatibility, and potential biosafety considerations. See also RecA, RAD51, homologous recombination, and synthetic biology.