Loading of PCNA - Sliding Clamp Formation on the C-strand of the telomere

Stable Identifier
R-HSA-174439
Type
Reaction [transition]
Species
Homo sapiens
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The binding of the primer recognition complex involves the loading of the proliferating cell nuclear antigen (PCNA). Replication Factor C (RFC) transiently opens the PCNA toroid in an ATP-dependent reaction, and then allows PCNA to re-close around the double helix adjacent to the primer terminus. This leads to the formation of the "sliding clamp" (Tsurimoto et al. 1990, Mossi and Hubscher 1998). In a human telomere replication model, RFC-mediated PCNA loading increases the processivity of telomeric C-strand synthesis, but does not eliminate polymerase delta stalling on the G-rich template (Lormand et al. 2013).
Interaction of RTEL1 with PCNA is needed for telomere replication and maintenance of telomere integrity (Vannier et al. 2013).

Literature References
PubMed ID Title Journal Year
24038470 DNA polymerase δ stalls on telomeric lagging strand templates independently from G-quadruplex formation

Lormand, JD, Buncher, N, Murphy, CT, Kaur, P, Lee, MY, Burgers, P, Wang, H, Kunkel, TA, Opresko, PL

Nucleic Acids Res. 2013
24115439 RTEL1 is a replisome-associated helicase that promotes telomere and genome-wide replication

Vannier, JB, Sandhu, S, Petalcorin, MI, Wu, X, Nabi, Z, Ding, H, Boulton, SJ

Science 2013
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Catalyst Activity
Title
DNA clamp loader activity of RFC Heteropentamer:RNA primer-DNA primer:G-strand extended telomere end [nucleoplasm]
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