DNA transposons facilitate the insertion of genetic fragments into diverse DNA sequences, enabling the generation of extensive mutant libraries. While transposition has traditionally been regarded as a DNA-based mechanism, recent advances have extended this concept to the protein level.
In a recent pioneering study, Hua et al. introduced a system for protein transposition, which enables the replacement of internal protein segments using artificial peptides-engineered split inteins. This molecular “cut-and-paste” approach allows precise editing of folded protein complexes, facilitating the incorporation of diverse noncoded elements. The method opens new avenues for probing and engineering protein function in both in vitro and cellular environments.
More Readings:
- A transposon-like strategy for proteins. Nat Chem Biol 21, 980–982 (2025). DOI:10.1038/s41589-025-01947-8
- Intracellular protein editing enables incorporation of noncanonical residues in endogenous proteins. Science. DOI: 10.1126/science.adr5499