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Article

Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate.

The Journal of biological chemistry - 26 Apr 2002

Kao Hui-I, Henricksen Leigh A, Liu Yuan, Bambara Robert A

Abstract excerpt

Flap endonuclease 1 (FEN1) is a structure-specific nuclease that cleaves substrates containing unannealed 5'-flaps during Okazaki fragment processing. Cleavage removes the flap at or near the point of annealing. The preferred substrate for archaeal FEN1 or the 5'-nuclease domains of bacterial DNA polymerases is a double-flap structure containing a 3'-tail on the upstream primer adjacent to the 5'-flap. We report...

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Source

Identifiers

PMID: 11825897
DOI: 10.1074/jbc.M110662200

Genes

FEN1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate.PMID 11825897Read ↗

Significance of the dissociation of Dna2 by flap endonuclease 1 to Okazaki fragment processing in Saccharomyces cerevisiae.Semantic proximity Read ↗

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Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathways.Semantic proximity Read ↗

Processing of branched DNA intermediates by a complex of human FEN-1 and PCNASemantic proximity Read ↗

The flexible loop of human FEN1 endonuclease is required for flap cleavage during DNA replication and repair.Semantic proximity Read ↗

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