Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51
Description
During homologous recombination, Rad51 forms a nucleoprotein filament on single-stranded DNA to promote DNA strand exchange. This filament binds to double-stranded DNA (dsDNA), searches for homology, and promotes transfer of the complementary strand, producing a new heteroduplex. Strand exchange proceeds via two distinct three-strand intermediates, C1 and C2. C1 contains the intact donor dsDNA whereas C2 contains newly formed heteroduplex DNA. Here, we show that the conserved DNA binding motifs, loop 1 (L1) and loop 2 (L2) in site I of Rad51, play distinct roles in this process. L1 is involved in formation of the C1 complex whereas L2 mediates the C1–C2 transition, producing the heteroduplex. Another DNA binding motif, site II, serves as the DNA entry position for initial Rad51 filament formation, as well as for donor dsDNA incorporation. Our study provides a comprehensive molecular model for the catalytic process of strand exchange mediated by eukaryotic RecA-family recombinases.
identifier:oai:t2r2.star.titech.ac.jp:50586007
Journal
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- Nature Communications
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Nature Communications 11 (No. 1), 1-, 2020-06
Nature Research
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Keywords
- DNA Repair
- DNA recombination
- Science
- DNA, Single-Stranded
- Saccharomyces cerevisiae
- Protein Structure, Secondary
- Article
- Adenosine Triphosphate
- Schizosaccharomyces
- Humans
- Homologous Recombination
- Binding Sites
- Q
- DNA damage and repair
- Nucleic Acid Heteroduplexes
- DNA
- Mutation
- Enzyme mechanisms
- Rad51 Recombinase
- DNA Damage
Details 詳細情報について
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- CRID
- 1050288757460560768
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- NII Article ID
- 120007117439
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- ISSN
- 20411723
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- PubMed
- 32528002
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- Crossref
- CiNii Articles
- KAKEN
- OpenAIRE