PolyADP-ribosylation articles from across Nature Portfolio

Here the authors identify that PARP1 maintains genome integrity by regulating replication fork recovery by break-induced replication. Mechanistically, this is achieved through MRE11-dependent PARP1 activation and site-specific ADP-ribosylation of PolD3.

SET8 is post-translationally poly ADPribosylated by PARP1 on several lysine residues, leading to SET8 degradation via ubiquitylation and genome-wide aberrant H4K20 methylation.

Structural insights into the poly-ADP-ribosyltransferase tankyrase reveal its filamentous architecture and illustrate how assembly controls catalytic and non-catalytic functions.

García Saura et al. report a new tool, MacroGreen, to detect ADP-ribosylation by GFP fluorescence in a microplate reader, or in cells by microscopy. With superior affinity and reduced ADP-ribosyl hydrolase activity, MacroGreen is an easy to produce and suitable tool for rapid detection of ADP-ribosylated proteins in vitro without a need for specialist reagents and time-consuming methods.

The use of a chemical genetics approach to identify poly(ADP-ribose) polymerase (PARP) targets revealed that PARP1 promotes transcription elongation.

Macrodomains are conserved globular domains that can interact with, and in some cases modify, ADP-ribose–based molecules. In this issue, two reports add to the functional repertoire of this domain, by demonstrating that a subset of macrodomain-containing proteins functions to catalyze the removal of protein-proximal ADP-ribose.