The interaction of ImuB with the β sliding clamp is essential for induced mutagenesis in mycobacteria and could be a novel target for new anti-tuberculosis drugs designed to inhibit the emergence of genetic resistance.

X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.

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.

The nuclease of hDNA2 limits its processive DNA unwinding capacity; the helicase function becomes stimulatory when hDNA2 is in complex with BLM or WRN helicase to degrade dsDNA.

Genetic and biochemical analyses reveal an important role for the translesion DNA polymerase DinB2 in mycobacterial mutagenesis, including in the insertion/deletion events that are an increasingly recognized type of diversity in Mycobacterium tuberculosis genomes.

DynAPs are liquid-like organelles that are partitioned into functional sub-domains.

Replication stress induces phosphorylation events within RIF1 intrinsically disordered region that are essential for RIF1's role in DNA replication fork protection.

Replication-transcription conflicts cause pervasive replisome instability.

Structural characterization of human RPA70N association with a series of DNA damage response proteins reveals versatile protein interaction mechanisms that help to recruit DNA repair proteins to the damage site quickly and efficiently.