Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases.

@article{Yao1996ClampLU,
  title={Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases.},
  author={Nina Y. Yao and Jeremy Turner and Zvi Kelman and Peter T. Stukenberg and Frank B. Dean and David Shechter and Z. Q. Pan and Jerard Hurwitz and Mike O'Donnell},
  journal={Genes to cells : devoted to molecular & cellular mechanisms},
  year={1996},
  volume={1 1},
  pages={101-13}
}
BACKGROUND The high speed and processivity of replicative DNA polymerases reside in a processivity factor which has been shown to be a ring-shaped protein. This protein ("sliding clamp') encircles DNA and tethers the catalytic unit to the template. Although in eukaryotic, prokaryotic and bacteriophage-T4 systems, the processivity factors are ring-shaped, they assume different oligomeric states. The Escherichia coli clamp (the beta subunit) is active as a dimer while the eukaryotic and T4 phage… CONTINUE READING
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