Coordinated DNA Replication by the Bacteriophage T4 Replisome
The T4 bacteriophage encodes eight proteins, which are sufficient to carry out coordinated leading and lagging strand DNA synthesis. These purified proteins have been used to reconstitute DNA synthesis in vitro and are a well-characterized model system. Recent work on the T4 replisome has yielded mo...
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| Format: | Online |
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MDPI
2015
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4488733/ |
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pubmed-4488733 |
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pubmed-44887332015-07-02 Coordinated DNA Replication by the Bacteriophage T4 Replisome Noble, Erin Spiering, Michelle M. Benkovic, Stephen J. Review The T4 bacteriophage encodes eight proteins, which are sufficient to carry out coordinated leading and lagging strand DNA synthesis. These purified proteins have been used to reconstitute DNA synthesis in vitro and are a well-characterized model system. Recent work on the T4 replisome has yielded more detailed insight into the dynamics and coordination of proteins at the replication fork. Since the leading and lagging strands are synthesized in opposite directions, coordination of DNA synthesis as well as priming and unwinding is accomplished by several protein complexes. These protein complexes serve to link catalytic activities and physically tether proteins to the replication fork. Essential to both leading and lagging strand synthesis is the formation of a holoenzyme complex composed of the polymerase and a processivity clamp. The two holoenzymes form a dimer allowing the lagging strand polymerase to be retained within the replisome after completion of each Okazaki fragment. The helicase and primase also form a complex known as the primosome, which unwinds the duplex DNA while also synthesizing primers on the lagging strand. Future studies will likely focus on defining the orientations and architecture of protein complexes at the replication fork. MDPI 2015-06-19 /pmc/articles/PMC4488733/ /pubmed/26102578 http://dx.doi.org/10.3390/v7062766 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Noble, Erin Spiering, Michelle M. Benkovic, Stephen J. |
| spellingShingle |
Noble, Erin Spiering, Michelle M. Benkovic, Stephen J. Coordinated DNA Replication by the Bacteriophage T4 Replisome |
| author_facet |
Noble, Erin Spiering, Michelle M. Benkovic, Stephen J. |
| author_sort |
Noble, Erin |
| title |
Coordinated DNA Replication by the Bacteriophage T4 Replisome |
| title_short |
Coordinated DNA Replication by the Bacteriophage T4 Replisome |
| title_full |
Coordinated DNA Replication by the Bacteriophage T4 Replisome |
| title_fullStr |
Coordinated DNA Replication by the Bacteriophage T4 Replisome |
| title_full_unstemmed |
Coordinated DNA Replication by the Bacteriophage T4 Replisome |
| title_sort |
coordinated dna replication by the bacteriophage t4 replisome |
| description |
The T4 bacteriophage encodes eight proteins, which are sufficient to carry out coordinated leading and lagging strand DNA synthesis. These purified proteins have been used to reconstitute DNA synthesis in vitro and are a well-characterized model system. Recent work on the T4 replisome has yielded more detailed insight into the dynamics and coordination of proteins at the replication fork. Since the leading and lagging strands are synthesized in opposite directions, coordination of DNA synthesis as well as priming and unwinding is accomplished by several protein complexes. These protein complexes serve to link catalytic activities and physically tether proteins to the replication fork. Essential to both leading and lagging strand synthesis is the formation of a holoenzyme complex composed of the polymerase and a processivity clamp. The two holoenzymes form a dimer allowing the lagging strand polymerase to be retained within the replisome after completion of each Okazaki fragment. The helicase and primase also form a complex known as the primosome, which unwinds the duplex DNA while also synthesizing primers on the lagging strand. Future studies will likely focus on defining the orientations and architecture of protein complexes at the replication fork. |
| publisher |
MDPI |
| publishDate |
2015 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4488733/ |
| _version_ |
1613242816944668672 |