An RNA enzyme is caught in the act of evolving a new structural domain within its active site, resulting in enhanced catalytic function.

A single human cell makes 10-100 transcriptional errors per second; these errors affect splicing and may influence the evolution of coding sequences.

Adopting RNA trinucleotides as substrates, ribozymes can catalyse the copying of structured RNA sequences, allowing self-synthesis by part of a newly evolved symbiotic ribozyme pair.

The roles of key telomerase active site residues were elucidated to determine how telomerase selects the correct from the incorrect nucleotide to maintain telomere integrity.

An RNA enzyme is shown to function as a reverse transcriptase, an activity thought to be crucial for the transition from RNA to DNA genomes during the early history of life on Earth.

Live-cell imaging shows that replication-independent specialized polymerase action is a consequence of lesion processing via NER and impacts cellular survival under stress outside replicative phases of the cell cycle.

Competing DNA polymerases at the DNA sliding clamp are revealed by single-molecule co-localization studies.

Polymerase θ is among the most proficient terminal transferases known and switches between three different mechanisms of terminal transferase activity.

Favipiravir, a novel nucleoside analogue, can clear a persistent norovirus infection in vivo through lethal mutagenesis.

All steps of a viroid-like replication cycle can be catalyzed by RNA alone.