Abstract
The field of DNA replication was launched upon discovery of the first DNA polymerase by Kornberg and Lehman (1, 2). DNA polymerase I displayed the novel and highly exciting property of template-directed enzymatic action, and like a split personality, DNApolymerase I could also degradeDNA, from either direction. Escherichia coli is now known to contain five different DNA polymerases. The chromosomal replicase is DNA polymerase III, while the damage-inducible DNA polymerases II, IV, and V play roles in DNA repair. DNA polymerase I is involved in both replication and repair and remains the most advanced model for the structure and function of DNA polymerase action. DNA polymerase III (pol III)2 functions in the context of a multiprotein apparatus called DNA pol III holoenzyme (reviewed in (3–5)). pol III holoenzyme contains 10 different proteins, which assort into three major functional units: 1) pol III core, 2) the sliding clamp, and 3) the / complex clamp loader. The holoenzyme contains two copies of the pol III core, which are connected by the attachment to one clamp loader. The holoenzyme functions within the context of a dynamic replisome containing pol III holoenzyme, a hexameric DnaB helicase, DnaGprimase, and SSB. During replisome function, contacts between these proteins are in a constant state of change. This review briefly summarizes the architecture and dynamic behavior of the E. coli replisome.
Highlights
Replisome Architecture and Dynamics in Escherichia coli*From the Laboratory of DNA Replication, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021
DNA polymerase III2 functions in the context of a multiprotein apparatus called DNA pol III holoenzyme. pol III holoenzyme contains 10 different proteins, which assort into three major functional units: 1) pol III core, 2) the  sliding clamp, and 3) the ␥/ complex clamp loader
The E. coli ␥ complex clamp loader contains five subunits that are essential for clamp loading activity, three ␥ protomers and one copy each of ␦ and ␦Ј
Summary
From the Laboratory of DNA Replication, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021. Escherichia coli is known to contain five different DNA polymerases. DNA polymerase I is involved in both replication and repair and remains the most advanced model for the structure and function of DNA polymerase action. DNA polymerase III (pol III) functions in the context of a multiprotein apparatus called DNA pol III holoenzyme (reviewed in [3,4,5]). Pol III holoenzyme contains 10 different proteins, which assort into three major functional units: 1) pol III core, 2) the  sliding clamp, and 3) the ␥/ complex clamp loader. The holoenzyme contains two copies of the pol III core, which are connected by the attachment to one clamp loader. The holoenzyme functions within the context of a dynamic replisome containing pol III holoenzyme, a hexameric DnaB helicase, DnaG primase, and SSB. This review briefly summarizes the architecture and dynamic behavior of the E. coli replisome
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
