Her lab was the first to use reverse-genetic approach to isolate the cDNA clones encoding the catalytic polypeptide of the principal chromosome replication initiation enzyme, DNA polymerase alpha, of human cells.
Significantly, analysis of the deduced amino-acid sequence of the human DNA polymerase alpha revealed six protein regions that are highly conserved in other family B DNA polymerases including yeast, bacteriophages T4, phage phi 29, herpes family viruses, vaccinia virus and adenovirus.
She used a model organism, fission yeast (Schizosaccharomyces pombe), taking a genetic, biochemical, and cell biology approach for the studies.
To prevent deleterious mutator phenotypes caused by defective replication proteins, cells activate a complex set of signal transduction response checkpoint pathway.
The checkpoint pathways regulate cell-cycle transition, induce tolerance by up-regulating and recruiting special polymerases (translesion polymerases) onto chromatin for mutagenic synthesis to tolerate the stress and to facilitate replication fork re-start, also can regulate an endonuclease to prevent deleterious genomic rearrangement, or in some cases to induce apoptosis.