DNA ligase I is recruited to sites of DNA replication by an interaction with proliferating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories.

@article{Montecucco1998DNALI,
  title={DNA ligase I is recruited to sites of DNA replication by an interaction with proliferating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories.},
  author={Alessandra Montecucco and Rossella Rossi and David S. Levin and R Gary and Min Sik Park and Teresa A. Motycka and Giovanni Ciarrocchi and Antonello Villa and Giuseppe Biamonti and Alan E. Tomkinson},
  journal={The EMBO journal},
  year={1998},
  volume={17 13},
  pages={3786-95}
}
In mammalian cells, DNA replication occurs at discrete nuclear sites termed replication factories. Here we demonstrate that DNA ligase I and the large subunit of replication factor C (RF-C p140) have a homologous sequence of approximately 20 amino acids at their N-termini that functions as a replication factory targeting sequence (RFTS). This motif consists of two boxes: box 1 contains the sequence IxxFF whereas box 2 is rich in positively charged residues. N-terminal fragments of DNA ligase I… CONTINUE READING
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