Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 21, Pages 7647-7652Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1321076111
Keywords
single-molecule techniques; DNA replication; DNA repair; lesion bypass; DinB
Categories
Funding
- National Institutes of Health [T32 GM008313, R01 GM066094, R01 CA021615, P30ES002019]
- National Science Foundation
- Smith Family Award in Biomedical Excellence
- Stuart Trust Fellows Award
- Australian Research Council [DP0877658]
- Australian Research Council [DP0877658] Funding Source: Australian Research Council
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Translesion synthesis (TLS) by Y-family DNA polymerases alleviates replication stalling at DNA damage. Ring-shaped processivity clamps play a critical but ill-defined role in mediating exchange between Y-family and replicative polymerases during TLS. By reconstituting TLS at the single-molecule level, we show that the Escherichia coli beta clamp can simultaneously bind the replicative polymerase (Pol) III and the conserved Y-family Pol IV, enabling exchange of the two polymerases and rapid bypass of a Pol IV cognate lesion. Furthermore, we find that a secondary contact between Pol IV and beta limits Pol IV synthesis under normal conditions but facilitates Pol III displacement from the primer terminus following Pol IV induction during the SOS DNA damage response. These results support a role for secondary polymerase clamp interactions in regulating exchange and establishing a polymerase hierarchy.
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