A modular approach to enzymatic ligation of peptides and proteins with oligonucleotides

A modular approach has been developed for enzymatic ligation of peptides/proteins with oligonucleotides through the design of tag phosphoramidites as adaptors, paving the way towards streamlined production of peptide/protein-oligonucleotide conjugates.

Assembly of a functional ribozyme from short oligomers by enhanced non-enzymatic ligation

The non-enzymatic replication of the primordial genetic material is thought to have enabled the evolution of the first ribozymes, leading to early forms of RNA-based life. However, the reported rate of chemical RNA ligation is extremely slow. Here we show that the rate of ligation can be greatly enhanced by employing a 3′-amino group at the 3′-end of each oligonucleotide, in combination with an N-alkyl imidazole organocatalyst. These modifications allow the rapid copying of long RNA templates by multi-step ligation of tetranucleotides, as well as the assembly of long oligonucleotides from short template splints. Our work shows that a functional RNA ligase ribozyme can be assembled from relatively short oligonucleotides, demonstrating a transition from non-enzymatic ligation to enzymatic ligation. We suggest that the genomes of primitive protocells could have consisted of relatively easily replicated oligonucleotides as short as 10 to 12 nucleotides in length.

Enhancing the stability of DNA origami nanostructures: staple strand redesign versus enzymatic ligation

Merging of bridging staples with adjacent oligonucleotide sequences leads to a moderate increase of DNA origami stability, while enzymatic ligation after assembly yields a reinforced nanostructure with superior stability at up to 37 °C and in the presence of 6 M urea.