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Article

A novel property of the RecA nucleoprotein filament: activation of double- stranded DNA for strand exchange in trans.

Genes & development - 1 Aug 1999

Mazin A V, Kowalczykowski S C

Abstract excerpt

RecA protein catalyzes DNA strand exchange, a basic step of homologous recombination. Upon binding to single-stranded DNA (ssDNA), RecA protein forms a helical nucleoprotein filament. Normally, this nucleoprotein filament binds double-stranded DNA (dsDNA) and promotes exchange of base pairs betwe...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 10444598
DOI: 10.1101/gad.13.15.2005
PMCID: PMC316918

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-10444598-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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A novel property of the RecA nucleoprotein filament: activation of double- stranded DNA for strand exchange in trans.PMID 10444598Read ↗

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Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein.Semantic proximity Read ↗

Helical interactions in homologous pairing and strand exchange driven by RecA protein.Semantic proximity Read ↗

Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament.Semantic proximity Read ↗

Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51.Semantic proximity Read ↗

Structural mechanism of strand exchange by the RAD51 filamentSemantic proximity Read ↗

Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant.Semantic proximity Read ↗

The mutant RecA proteins, RecAR243Q and RecAK245N, exhibit defective DNA binding in homologous pairing.Semantic proximity Read ↗

Dynamic formation of RecA filaments at DNA double strand break repair centers in live cells.Semantic proximity Read ↗

Human RAD51 rapidly forms intrinsically dynamic nucleoprotein filaments modulated by nucleotide binding state.Semantic proximity Read ↗

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