Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis
Name
Kath-2014-Polymerase exchange.pdf
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1.36 MB
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Adobe PDF
Checksum (MD5)
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Author(s)
Kath, James E.
Jergic, Slobodan
Heltzel, Justin M. H.
Jacob, Deena T.
Dixon, Nicholas E.
Sutton, Mark D.
Walker, Graham C.
Loparo, Joseph J.
Date Issued
May 2014
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publisher
National Academy of Sciences (U.S.)
Citation
Kath, J. E., S. Jergic, J. M. H. Heltzel, D. T. Jacob, N. E. Dixon, M. D. Sutton, G. C. Walker, and J. J. Loparo. “Polymerase Exchange on Single DNA Molecules Reveals Processivity Clamp Control of Translesion Synthesis.” Proceedings of the National Academy of Sciences 111, no. 21 (May 13, 2014): 7647–7652.
Version
Final published version
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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1073/pnas.1321076111
