Transcription factors can read out both the sequence and the structure of the non-template DNA strand in the transcription bubble, expanding the repertoire of mechanisms to control transcription.

The CMG complex, the replicative helicase in eukaryotes, uses a different mechanism from bacterial and viral helicases by engaging both strands of parental DNA with substantial force and unwinding the duplex within the central channel of CMG.

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

Structural and functional studies reveal how Newcastle disease virus nucleocapsid protects its viral genome through a self-capping mechanism, which is important for new antiviral drug design.

The crystal structure of the MCM helicase bound to single-stranded DNA reveals a binding motif that is critical for cell viability, helicase activation and DNA replication.

Structures of the replicative DNA polymerase Pol IIIα, the DNA sliding clamp, the proofreading exonuclease, and the processivity switch Tau (τ) suggest a mechanism for quick release during lagging strand synthesis.

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.

Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

A combination of genetics and biophysical approaches identifies an overlapping set of sequences that form non-canonical G-quadruplex structures in vitro and induce genomic instability in cells.

Biochemical data demonstrate an unexpected and critical function for the enigmatic Mcm10 protein in helping the eukaryotic CMG helicase/replisome bypass roadblocks on the DNA that may also explain Mcm10 function at origins of replication.