Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic ψχ heterodimer
Author:
Affiliation:
1. Biochemistry and Molecular Biology, University of Florida, P.O. BOX 100245, Gainesville, Florida 32610, USA
2. Cornell High Energy Synchrotron Source (CHESS), Cornell University, 161 Synchrotron Drive, Ithaca, New York 14853, USA
Publisher
AIP Publishing
Subject
Spectroscopy,Condensed Matter Physics,Instrumentation,Radiation
Link
http://scitation.aip.org/deliver/fulltext/aca/journal/sdy/2/5/1.4927407.pdf?itemId=/content/aca/journal/sdy/2/5/10.1063/1.4927407&mimeType=pdf&containerItemId=content/aca/journal/sdy
Reference50 articles.
1. DNA Replicases from a Bacterial Perspective
2. CELLULAR DNA REPLICASES: Components and Dynamics at the Replication Fork
3. Involvement of Two Protein Factors and ATP in In Vitro DNA Synthesis Catalyzed by DNA Polymerase III of Escherichia coli
4. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
5. A Sliding-Clamp Toolbelt Binds High- and Low-Fidelity DNA Polymerases Simultaneously
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3. DNA Recognition/Processing | DNA Polymerase III, Bacterial;Encyclopedia of Biological Chemistry III;2021
4. The inactivation ofrfaP,rarAorsspAgene improves the viability of theEscherichia coliDNA polymerase IIIholDmutant;Molecular Microbiology;2017-04-12
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