Topic
PCNA complex
About: PCNA complex is a research topic. Over the lifetime, 30 publications have been published within this topic receiving 3839 citations.
Papers
TL;DR: The crystal structure of the processivity factor required by eukaryotic DNA polymerase delta, proliferating cell nuclear antigen from S. cerevisiae, has been determined and the dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase.
952 citations
TL;DR: The ability to visualize repair intermediates in the absence of PCNA facilitates dissection of the multiprotein reaction that leads to incision of damaged DNA in a major pathway of cellular defense against mutagens.
849 citations
TL;DR: The immobilized template system was employed to address the biochemical mechanisms underlying the coordination between the various proteins required for nucleotide excision repair (NER), and it was found that PCNA and RF‐C arrival requires XPF 5′ incision and that this interaction with XPG protectsPCNA and Polδ from the effect of inhibitors such as p21.
Abstract: To address the biochemical mechanisms underlying the coordination between the various proteins required for nucleotide excision repair (NER), we employed the immobilized template system. Using either wild-type or mutated recombinant proteins, we identified the factors involved in the NER process and showed the sequential comings and goings of these factors to the immobilized damaged DNA. Firstly, we found that PCNA and RF-C arrival requires XPF 5′ incision. Moreover, the positioning of RF-C is facilitated by RPA and induces XPF release. Concomitantly, XPG leads to PCNA recruitment and stabilization. Our data strongly suggest that this interaction with XPG protects PCNA and Polδ from the effect of inhibitors such as p21. XPG and RPA are released as soon as Polδ is recruited by the RF-C/PCNA complex. Finally, a ligation system composed of FEN1 and Ligase I can be recruited to fully restore the DNA. In addition, using XP or trichothiodystrophy patient-derived cell extracts, we were able to diagnose the biochemical defect that may prove to be important for therapeutic purposes.
173 citations
TL;DR: It is proposed that p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.
Abstract: The intrinsically disordered protein p15(PAF) regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15(PAF)-PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15(PAF) tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15(PAF) also contacts the inside of, and passes through, the PCNA ring. The disordered p15(PAF) termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15(PAF) binds DNA mainly through its histone-like N-terminal tail, while PCNA does not, and a model of the ternary complex with DNA inside the PCNA ring is consistent with electron micrographs. We propose that p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.
80 citations
TL;DR: The crystal structure of PCNA in complex with a non-canonical PCNA-interacting motif in Pif1 is solved and provides insights into the role of the Pif 1-PCNA-Pol δ ensemble during DNA break repair by homologous recombination.
76 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 2 |
| 2018 | 1 |
| 2017 | 2 |
| 2015 | 1 |
| 2010 | 1 |
| 2008 | 2 |