Archaeal DNA Polymerases: Enzymatic Abilities, Coordination, and Unique Properties

Abstract

DNA polymerases from archaea coordinate both replication and repair activities under extreme conditions. Traditional DNA polymerase families B and Y are represented, but an entire phylum of archaea contains members from the unique D-family. These model archaeal polymerases from each family have be exploited for a variety of biotechnology applications but have also provided great insight into kinetic mechanisms, structural properties, conformational changes, and protein interactions with DNA polymerases from other domains. Interestingly, individual polymerase members have revealed some unique features including template uracil recognition, more open active sites, novel motifs, and direct polymerase interactions that modulate replication and repair in these simpler organisms. How multiple polymerases coordinate synthesis on the leading and lagging strands and replication or repair duties is an ongoing fundamental question in archaea. Nevertheless, their intrinsic enzymatic properties are fascinating and continue to shape and influence research avenues for all DNA polymerases. The ability to regulate robust and accurate DNA synthesis through specific and loosely associate oligomeric states and protein interactions maintains a high degree of genomic stability in spite of harsh environmental conditions.