Removal of remaining Flap from the C-strand

Stable Identifier
Reaction [transition]
Homo sapiens
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The remaining flap, which is too short to support RPA binding, is then processed by FEN1. There is evidence that binding of RPA to the displaced end of the RNA-containing Okazaki fragment prevents FEN1 from accessing the substrate. FEN1 is a structure-specific endonuclease that cleaves near the base of the flap at a position one nucleotide into the annealed region. Biochemical studies have shown that the preferred substrate for FEN1 consists of a one-nucleotide 3'-tail on the upstream primer in addition to the 5'-flap of the downstream primer (Harrington and Lieber 1994, Harrington and Lieber 1995, Murante et al. 1996, Lieber 1997, Kaiser et al. 1999, Xu et al. 2000, Kao et al. 2002). The interaction of FEN1 with WRN, a RECQ family DNA helicase, is needed for successful flap cleavage during telomeric strand displacement synthesis (Saharia et al. 2010, Li et al. 2017).
Literature References
PubMed ID Title Journal Year
20551483 FEN1 ensures telomere stability by facilitating replication fork re-initiation

Chiappinelli, KB, Teasley, DC, Saharia, A, Dao, B, Stewart, SA, Duxin, JP

J. Biol. Chem. 2010
27849570 The Werner Syndrome Helicase Coordinates Sequential Strand Displacement and FEN1-Mediated Flap Cleavage during Polymerase δ Elongation

Reddy, S, Li, B, Comai, L

Mol. Cell. Biol. 2017
Event Information
Catalyst Activity

5'-flap endonuclease activity of FEN1 [nucleoplasm]

This event is regulated
Positively by
Orthologous Events
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