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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Reddy, M. K. Von Hippel, P. H. Weitzel, S. E. |
Description | Author Affiliation: Reddy MK ( Institute of Molecular Biology, University of Oregon, Eugene 97403.); |
Abstract | The seven-protein bacteriophage T4 DNA replication complex can be manipulated in vitro to study mechanistic aspects of the elongation phase of DNA replication. Under physiological conditions, the processivity of DNA synthesis catalyzed by the T4 polymerase (gp43) is greatly increased by the interaction of this enzyme with its accessory proteins (gp44/62 and gp45) and the T4 single-stranded DNA binding protein (gp32). The assembly of this T4 holoenzyme requires hydrolysis of ATP by the gp44/62 complex. We demonstrate here that processive T4 holoenzyme-like DNA synthesis can be obtained without hydrolysis of ATP by simply adding gp45 to the T4 DNA polymerase at extremely high concentrations, effectively bypassing the ATPase subunits (gp44/62) of the accessory protein complex. The amount of gp45 required for the gp43-gp45 heteroassociation event is reduced by addition of the macromolecular crowding agent polyethylene glycol (PEG) as well as gp32. A chromatographic strategy involving PEG has been used to demonstrate the gp43-gp45 interaction. These results suggest that gp45 is ultimately responsible for increasing the processivity of DNA synthesis via a direct and functionally significant interaction with the T4 DNA polymerase. A corollary to this notion is that the specific role of the gp44/62 complex is to catalytically link gp45 to gp43. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 8 |
Volume Number | 90 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 1993-05-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Bacteriophage T4 Genetics Metabolism DNA Replication DNA, Viral DNA-Directed DNA Polymerase Trans-Activators Viral Proteins Adenosine Triphosphate Chromatography, Affinity Coliphages DNA-Binding Proteins Isolation & Purification Escherichia Coli Kinetics Molecular Sequence Data Oligodeoxyribonucleotides Templates, Genetic Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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