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DNA repair enzymes are enzymes that recognize and correct physical damage in DNA, caused by exposure to radiation, UV light or reactive oxygen species. The correction of DNA damage alleviates loss of genetic information, generation of double-strand breaks, and DNA crosslinkages. DNA repair enzymes recognize DNA damage or a nearby site, or enable repair.
Replicative sliding clamp loading is critical for DNA replication and repair. Here, authors report structures of major clamp loading intermediates in a bacterial system, revealing how the clamp is opened and loaded onto DNA.
Formation of biomolecular condensate via liquid-like assembly of PARylated PARP1 is driven by biogenic cations. This assembly regulates autoPARylation of PARP1, PARG-dependent hydrolysis of poly(ADP-ribose) and Polβ-mediated DNA synthesis.
Using highly purified protein factors, we provide evidence that BRCA1–BARD1 physically interacts with EXO1, BLM and WRN and upregulates the activity of all three resection pathways.
Antibody diversification relies on the intentional mutagenesis of immunoglobulin genes for adaptive immune responses. Here, the authors identified a CTLH E3 ubiquitin ligase complex that co-opts FAM72A to recruit and degrade the UNG2 base excision repair factor to permit mutagenesis.
RNase H1 functions as an endonuclease degrading the RNA moiety within RNA–DNA hybrids. Here the authors find that RNase H1 displays 3′-to-5′ exonuclease activity. Moreover, RPA reinforces RNase H1’s 3′-to-5′ nucleolytic rate and processivity and stimulates its 5′-to-3′ exonuclease activity.
Aitken et al. have used mutagen-induced liver tumours to trace individual strands of the DNA double helix to which damage occurred and correlate this with mutational patterns to inform upon tumour evolution.