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Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis

Journal Article


Abstract


  • 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 β 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 β 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.

Authors


  •   Kath, James E. (external author)
  •   Jergic, Slobodan
  •   Heltzel, Justin M. H. (external author)
  •   Jacob, Deena T. (external author)
  •   Dixon, Nicholas E.
  •   Sutton, Mark D. (external author)
  •   Walker, Graham C. (external author)
  •   Loparo, Joseph J. (external author)

Publication Date


  • 2014

Citation


  • Kath, J. E., Jergic, S., Heltzel, J. M. H., Jacob, D. T., Dixon, N. E., Sutton, M. D., Walker, G. C. & Loparo, J. J. (2014). Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis. Proceedings of the National Academy of Sciences of USA, 111 (21), 7647-7652.

Scopus Eid


  • 2-s2.0-84901660107

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/1787

Has Global Citation Frequency


Number Of Pages


  • 5

Start Page


  • 7647

End Page


  • 7652

Volume


  • 111

Issue


  • 21

Place Of Publication


  • United States

Abstract


  • 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 β 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 β 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.

Authors


  •   Kath, James E. (external author)
  •   Jergic, Slobodan
  •   Heltzel, Justin M. H. (external author)
  •   Jacob, Deena T. (external author)
  •   Dixon, Nicholas E.
  •   Sutton, Mark D. (external author)
  •   Walker, Graham C. (external author)
  •   Loparo, Joseph J. (external author)

Publication Date


  • 2014

Citation


  • Kath, J. E., Jergic, S., Heltzel, J. M. H., Jacob, D. T., Dixon, N. E., Sutton, M. D., Walker, G. C. & Loparo, J. J. (2014). Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis. Proceedings of the National Academy of Sciences of USA, 111 (21), 7647-7652.

Scopus Eid


  • 2-s2.0-84901660107

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/1787

Has Global Citation Frequency


Number Of Pages


  • 5

Start Page


  • 7647

End Page


  • 7652

Volume


  • 111

Issue


  • 21

Place Of Publication


  • United States