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Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA

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Sigurdsson, Stefan, Trujillo, Kelly, Song, BinWei, Stratton, Sabrina, Sung, Patrick·2001·Journal of Biological Chemistry

Abstract

Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.

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Research works printed but not linked: 17

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Metadata

Authors
Sigurdsson, S., Trujillo, K., Song, B., Stratton, S., & Sung, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-03
Volume
276
Issue
12
Pages
8798-8806
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1964702635
Cited by
172
References
2
FWCI
4.78
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA. https://app.cochat.ai/papers/10.1074/jbc.m010011200
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Sigurdsson, S., Trujillo, K., Song, B., Stratton, S., & Sung, P. (2001). Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m010011200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.