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Article

DNA binding by the substrate specificity (wedge) domain of RecG helicase suggests a role in processivity.

The Journal of biological chemistry - 8 Apr 2005

Briggs Geoffrey S, Mahdi Akeel A, Wen Qin, Lloyd Robert G

Abstract excerpt

RecG differs from most helicases acting on branched DNA in that it is thought to catalyze unwinding via translocation of a monomer on dsDNA, with a wedge domain facilitating strand separation. Conserved phenylalanines in the wedge are shown to be critical for DNA binding. When detached from the helicase domains, the wedge bound a Holliday junction with high affinity but failed to bind a replication fork...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15695524
DOI: 10.1074/jbc.M412054200

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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.

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