DNA articles from across Nature Portfolio

Coordinating the activities of replicative helicase and DNA polymerase(s) is crucial for DNA replication. Here, the authors show that DNA translocation by CMG is synchronized with the activities of Polε in the leading-strand replisome.

Limited delivery of therapeutic cells to diseased tissue hampers the effective application of mesenchymal stromal cells (MSCs). Here, authors modify the cell surface with polyvalent antibodies using DNA-templated assembly, and show that polyvalent interactions can be used to improve the targeting efficiency of MSCs.

The discovery of biomarkers remains challenging owing to a lack of methods sensitive enough to identify such rare molecules. Now, by simultaneously exploiting the catalysis and affinity of a DNAzyme, candidate biomarkers with low abundance in cancers can be pulled down for identification and validation.

Here, using cryo-EM, the authors show how Cas1–Cas2/3 and integration host factor, by means of a U-shaped bend that traps the invading DNA and a loop that positions it for the integrase, regulate integration of foreign DNA into the first repeat of the CRISPR array.

The nuclear envelope participates in the spatial regulation of DNA repair, but the mechanisms behind this are unclear. A study now reports that a nuclear envelope-localized nuclease, NUMEN/ENDOD1, guides the choice of DNA-repair pathway by inhibiting the resection of DNA ends and aberrant recombination, ensuring genome stability.

The mechanisms responsible for replicative misincorporation of an adenine into DNA opposite 8-oxoguanine (8OG) remain obscure. A new study suggests that 8OG redistributes the balance between several mispair conformations, enabling the high rates of misincorporation of adenine paired with 8OG by DNA polymerases.

Nanomachines are central to life and are becoming an important part of self-regulated nanotechnologies. Inspired by natural self-assembled nanosystems, it has been shown that artificial nanosystems can evolve and adopt regulatory functions upon fragmentation of their structures into multiple components that reassemble to form the same nanostructure.

Etoposide, a chemotherapeutic poison of type IIA eukaryotic topoisomerases (topo IIs), promotes topo II to compact DNA by trapping DNA loops, creates DNA double-strand breaks, causes topo II to resist relocation, and pauses the ability of topoisomerases to relax DNA supercoiling. Through these mechanisms, etoposide converts topo II into a roadblock to DNA processing.