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Similarity of the Yeast RAD51 Filament to the Bacterial RecA Filament

Ogawa, Tomoko, Yu, Xiong, Shinohara, Akira, Egelman, Edward H.·1993·Science

Abstract

The RAD51 protein functions in the processes of DNA repair and in mitotic and meiotic genetic recombination in the yeast Saccharomyces cerevisiae . The protein has adenosine triphosphate-dependent DNA binding activities similar to those of the Escherichia coli RecA protein, and the two proteins have 30 percent sequence homology. RAD51 polymerized on double-stranded DNA to form a helical filament nearly identical in low-resolution, three-dimensional structure to that formed by RecA. Like RecA, RAD51 also appears to force DNA into a conformation of approximately a 5.1-angstrom rise per base pair and 18.6 base pairs per turn. As in other protein families, its structural conservation appears to be stronger than its sequence conservation. Both the structure of the protein polymer formed by RecA and the DNA conformation induced by RecA appear to be general properties of a class of recombination proteins found in prokaryotes as well as eukaryotes.

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Metadata

Authors
Ogawa, T., Yu, X., Shinohara, A., & Egelman, E. H.
Venue
Science
Published
1993-03-26
Volume
259
Issue
5103
Pages
1896-1899
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2028084970
Cited by
670
References
0
FWCI
13.86
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Similarity of the Yeast RAD51 Filament to the Bacterial RecA Filament. https://app.cochat.ai/papers/10.1126/science.8456314
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Ogawa, T., Yu, X., Shinohara, A., & Egelman, E. H. (1993). Similarity of the Yeast RAD51 Filament to the Bacterial RecA Filament. Science. https://doi.org/10.1126/science.8456314

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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.