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Article

Dna2 exhibits a unique strand end-dependent helicase function.

The Journal of biological chemistry - 10 Dec 2010

Balakrishnan Lata, Polaczek Piotr, Pokharel Subhash, Campbell Judith L, Bambara Robert A

Abstract excerpt

Dna2 endonuclease/helicase participates in eukaryotic DNA transactions including cleavage of long flaps generated during Okazaki fragment processing. Its unusual substrate interaction consists of recognition and binding of the flap base, then threading over the 5'-end of the flap, and cleaving periodically to produce a terminal product ∼5 nt in length. Blocking the 5'-end prevents cleavage. The Dna2 ATP-driven 5'...

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Identifiers

PMID: 20929864
DOI: 10.1074/jbc.M110.165191
PMCID: PMC2998112

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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