DNA polymerases are essential enzymes responsible for replication and repair of DNA in all organisms. To replicate DNA with high fidelity, DNA polymerases must select the correct incoming nucleotide substrate during each cycle of nucleotide incorporation, in accordance with the templating base. When an incorrect nucleotide is sometimes inserted, the polymerase uses a separate 3′→5′ exonuclease to remove the misincorporated base (proofreading). Large conformational rearrangements of the polymerase–DNA complex occur during both the nucleotide incorporation and proofreading steps. Single-molecule fluorescence spectroscopy provides a unique tool for observation of these dynamic conformational changes in real-time, without the need to synchronize a population of DNA–protein complexes.
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April 2011
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Conference Article|
March 22 2011
DNA polymerase activity at the single-molecule level
Joshua P. Gill;
Joshua P. Gill
1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, U.S.A.
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Jun Wang;
Jun Wang
1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, U.S.A.
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David P. Millar
David P. Millar
1
1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, U.S.A.
1To whom correspondence should be addressed (email millar@scripps.edu).
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Publisher: Portland Press Ltd
Received:
September 06 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (2): 595–599.
Article history
Received:
September 06 2010
Citation
Joshua P. Gill, Jun Wang, David P. Millar; DNA polymerase activity at the single-molecule level. Biochem Soc Trans 1 April 2011; 39 (2): 595–599. doi: https://doi.org/10.1042/BST0390595
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