摘要：AbstractHuman exonuclease1 (hExo1) function in different processes of DNA metabolism which includes DNA replication and repair. Characterization of Exo1 has been most focused on the yeast homologue. The full-length human exonuclease1 has only been partially characterized. We report here, the biochemical studies on the full-length hExo1. We show that the stability and resection activity of hExo1 are affected by factors such as ionic strength, pH, and temperature. We determined the substrate preference of hExo1 by assaying its resection activity on different types of DNA substrates, our result show that hExo1 preferably degrades 3’ overhang dsDNA substrate, suggesting the preference of hExo1 resection activity to 3’ overhang dsDNA substrate.
