Processivity clamps are essential cofactors in DNA replication and are structurally and functionally conserved throughout evolution. These ring-shaped proteins encircle DNA and increase the processivity of DNA polymerases by tethering them to DNA. Processivity clamps also serve as hubs for protein-protein interactions as they interact with many proteins that regulate replication, DNA repair, translesion synthesis, and the cell cycle. Although multiple studies have probed the three-dimensional structure of various processivity clamps, less in known about their conformational dynamics in solution. In this research we use hydrogen exchange mass spectrometry to probe the conformational dynamics of processivity clamps from various sources, ranging from bacteriophage to humans. Our observations reveal that processivity clamps from different sources show a wide variety of dynamic behavior and that the highly conserved tertiary structure does not correlate with the conformational dynamics of the proteins.

Conformational analysis of processivity clamps demonstrates that tertiary structure does not correlate with dynamics

244th National Meeting (2012)

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