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Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea
The ability of the replisome to seamlessly coordinate both high fidelity and translesion DNA synthesis requires a means to regulate recruitment and binding of enzymes from solution. Co-occupancy of multiple DNA polymerases within the replisome has been observed primarily in bacteria and is regulated...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5737361/ https://www.ncbi.nlm.nih.gov/pubmed/28655184 http://dx.doi.org/10.1093/nar/gkx539 |
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author | Cranford, Matthew T. Chu, Aurea M. Baguley, Joshua K. Bauer, Robert J. Trakselis, Michael A. |
author_facet | Cranford, Matthew T. Chu, Aurea M. Baguley, Joshua K. Bauer, Robert J. Trakselis, Michael A. |
author_sort | Cranford, Matthew T. |
collection | PubMed |
description | The ability of the replisome to seamlessly coordinate both high fidelity and translesion DNA synthesis requires a means to regulate recruitment and binding of enzymes from solution. Co-occupancy of multiple DNA polymerases within the replisome has been observed primarily in bacteria and is regulated by posttranslational modifications in eukaryotes, and both cases are coordinated by the processivity clamp. Because of the heterotrimeric nature of the PCNA clamp in some archaea, there is potential to occupy and regulate specific polymerases at defined subunits. In addition to specific PCNA and polymerase interactions (PIP site), we have now identified and characterized a novel protein contact between the Y-family DNA polymerase and the B-family replication polymerase (YB site) bound to PCNA and DNA from Sulfolobus solfataricus. These YB contacts are essential in forming and stabilizing a supraholoenzyme (SHE) complex on DNA, effectively increasing processivity of DNA synthesis. The SHE complex can not only coordinate polymerase exchange within the complex but also provides a mechanism for recruitment of polymerases from solution based on multiequilibrium processes. Our results provide evidence for an archaeal PCNA ‘tool-belt’ recruitment model of multienzyme function that can facilitate both high fidelity and translesion synthesis within the replisome during DNA replication. |
format | Online Article Text |
id | pubmed-5737361 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-57373612018-01-08 Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea Cranford, Matthew T. Chu, Aurea M. Baguley, Joshua K. Bauer, Robert J. Trakselis, Michael A. Nucleic Acids Res Genome Integrity, Repair and Replication The ability of the replisome to seamlessly coordinate both high fidelity and translesion DNA synthesis requires a means to regulate recruitment and binding of enzymes from solution. Co-occupancy of multiple DNA polymerases within the replisome has been observed primarily in bacteria and is regulated by posttranslational modifications in eukaryotes, and both cases are coordinated by the processivity clamp. Because of the heterotrimeric nature of the PCNA clamp in some archaea, there is potential to occupy and regulate specific polymerases at defined subunits. In addition to specific PCNA and polymerase interactions (PIP site), we have now identified and characterized a novel protein contact between the Y-family DNA polymerase and the B-family replication polymerase (YB site) bound to PCNA and DNA from Sulfolobus solfataricus. These YB contacts are essential in forming and stabilizing a supraholoenzyme (SHE) complex on DNA, effectively increasing processivity of DNA synthesis. The SHE complex can not only coordinate polymerase exchange within the complex but also provides a mechanism for recruitment of polymerases from solution based on multiequilibrium processes. Our results provide evidence for an archaeal PCNA ‘tool-belt’ recruitment model of multienzyme function that can facilitate both high fidelity and translesion synthesis within the replisome during DNA replication. Oxford University Press 2017-08-21 2017-06-26 /pmc/articles/PMC5737361/ /pubmed/28655184 http://dx.doi.org/10.1093/nar/gkx539 Text en © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Genome Integrity, Repair and Replication Cranford, Matthew T. Chu, Aurea M. Baguley, Joshua K. Bauer, Robert J. Trakselis, Michael A. Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea |
title | Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea |
title_full | Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea |
title_fullStr | Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea |
title_full_unstemmed | Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea |
title_short | Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea |
title_sort | characterization of a coupled dna replication and translesion synthesis polymerase supraholoenzyme from archaea |
topic | Genome Integrity, Repair and Replication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5737361/ https://www.ncbi.nlm.nih.gov/pubmed/28655184 http://dx.doi.org/10.1093/nar/gkx539 |
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