The details of how the enzyme DNA polymerase α initiates the polymerization of nucleotides in DNA replication, a critical step in the synthesis of new chromosomal DNA, have been revealed in atomic detail.

Insight into the mechanism of DNA synthesis is provided by the crystal structures of DNA polymerase intermediates.

DNA synthesis by DNA polymerase V is regulated by an intrinsic DNA-dependent ATPase activity which has not been observed for any other polymerase.

The primer extension and 5' flap processing activities of DNA polymerase I are physically coordinated by combined movements of the DNA substrate and the 5' nuclease domain of the enzyme.

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.

Fluorescence resonance energy transfer has been used to explore the interactions between DNA polymerases, sliding clamps and clamp loaders as DNA is replicated in human cells.

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.

Translesion polymerase kappa promotes replication fork restart to maintain genome stability during conditions of nucleotide deprivation.

A detailed model of the T7 replisome with the precise positions of the helicase and polymerase at the replication fork explains how catalysis by the two enzymes is coordinated.

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