M Y Torgov

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The clamp loader complex (CLC) of bacteriophage T4 is essential for viability and has analogs in both prokaryotes and eukaryotes. The gp44 and gp62 subunits of the T4 CLC, in a 4:1 ratio, tightly associate such that the two proteins co-purify. Using transformed Escherichia coli, we were able to demonstrate for the first time purification of the unique(More)
The bacteriophage T4 DNA polymerase holoenzyme is composed of the core polymerase, gene product 43 (gp43), in association with the "sliding clamp" of the T4 system, gp45. Sliding clamps are the processivity factors of DNA replication systems. The T4 sliding clamp comes to encircle DNA via the "clamp loader" activity inherent in two other T4 proteins: 44 and(More)
Proper formation of the bacteriophage T4 DNA polymerase holoenzyme requires a wide spectrum of protein-protein and protein-DNA interactions among the DNA polymerase gp43, the sliding clamp gp45, and gp44/62, the clamp loader complex (CLC). The 44 and 62 proteins associate to form a tight complex maintained in a 4:1 ratio. The 44 and 62 genes are adjacent to(More)
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