Removal of remaining Flap

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 FEN-1. There is evidence that binding of RPA to the displaced end of the RNA-containing Okazaki fragment prevents FEN-1 from accessing the substrate. FEN-1 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 FEN-1 consists of a one-nucleotide 3'-tail on the upstream primer in addition to the 5'-flap of the downstream primer.

Literature References
PubMed ID Title Journal Year
8131753 The characterization of a mammalian DNA structure-specific endonuclease.

Harrington, JJ, Lieber, MR

EMBO J 1994
7876218 DNA structural elements required for FEN-1 binding.

Harrington, JJ, Lieber, MR

J Biol Chem 1995
Catalyst Activity

5'-flap endonuclease activity of FEN1 [nucleoplasm]

Orthologous Events
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