M. E. O'Donnell

The paper shows that single point mutations can restore function to a defective DNA polymerase clamp-loader complex by compensating for reduced affinity between the clamp loader and the sliding clamp.

This study uses cryo-EM to analyze the structural dynamics of yeast Pol α-primase during primer synthesis, revealing how RNA primers are transferred to DNA polymerase and how primer length is regulated.

This paper reports high-resolution structures of Rad24-RFC loading 9-1-1 onto DNA gaps, showing preference for ssDNA gaps and revealing a unique mechanism for clamp loading and DNA repair.

This paper reveals the mechanism by which Rad24-RFC loads the 9-1-1 clamp onto DNA by inserting ssDNA from the top of an open ring, differing from RFC/PCNA loading.

This study shows that the yeast origin recognition complex can bind nucleosomes and license replication origins without requiring a consensus DNA sequence, suggesting this mechanism is conserved across eukaryotes.

The paper identifies a hydrogen-bonded junction in DNA polymerase clamp loaders that is critical for allosteric communication, preserved across diverse AAA+ ATPases.

The paper provides evidence that CMG complexes unwind DNA by shearing it apart while binding only one strand, using an origin mimic DNA with specific structural features.

The paper shows Ctf4 organizes sister replisomes and Pol alpha into a replication factory by dimerizing CMG helicase and binding one Pol-primase.

The paper shows how DNA polymerase stability and exchange dynamics in the yeast replisome are tuned by local concentrations, enabling efficient replication and adaptation to genomic challenges.

The paper shows CMG helicase opens a single-stranded DNA gate to traverse forked junctions and resume replication after DNA damage, with Mcm10 facilitating this process.

This study shows Mcm10 enables CMG helicase to bypass DNA blocks on the non-tracking strand by isomerizing the CMG-DNA complex.