The discovery of a biomolecular condensate involved in DNA replication has wide ranging implications.

Two related DNA replication initiation proteins contribute to the decision of whether to enter a new round of the cell division cycle or enter into a period of proliferative quiescence.

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.

The discovery of a mechanism that causes DNA deletions during non-canonical DNA replication termination is described.

A mathematical model that combines stochasticity and spatial structure describes the dynamics of the viral population during an infection cycle, and fitting the model to RNA and virus abundances over time shows that poliovirus follows a geometric replication mode.

The universal eukaryotic DNA replication kinetics is the consequence of simple physicochemical rules resulting from the localisation of potential replication origins at discrete sites and the diffusion of limiting origin firing factors in the nuclear space.

Cryo-electron tomography unveils striking new structural components of positive-strand virus RNA replication compartments, greatly advancing mechanistic insights into the structure, assembly, function and control of these critical complexes.

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.

Transposition reactions that occur during DNA replication and involve the termini of adjacent transposons can induce genome expansion by re-replication of transposon-flanking sequences.

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.