Michael E. O’Donnell

Nov 8, 2024 | nature.com | Qing He |Feng Wang |Michael E. O’Donnell

Correction to: Nature Communications https://doi.org/10.1038/s41467-024-52257-x, published online 08 September 2024In the original version of the published article, the Supplementary Information was missing Supplementary Fig. 9. This has now been replaced.

Sep 8, 2024 | nature.com | Qing He |Feng Wang |Michael E. O’Donnell

AbstractIn eukaryotes, the leading strand DNA is synthesized by Polε and the lagging strand by Polδ. These replicative polymerases have higher processivity when paired with the DNA clamp PCNA. While the structure of the yeast Polε catalytic domain has been determined, how Polε interacts with PCNA is unknown in any eukaryote, human or yeast. Here we report two cryo-EM structures of human Polε–PCNA–DNA complex, one in an incoming nucleotide bound state and the other in a nucleotide exchange state.

Jun 13, 2024 | nature.com | Michael E. O’Donnell

AbstractHumans have three different proliferating cell nuclear antigen (PCNA) clamp-loading complexes: RFC and CTF18-RFC load PCNA onto DNA, but ATAD5-RFC can only unload PCNA from DNA. The underlying structural basis of ATAD5-RFC unloading is unknown.