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Article

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

Nature communications - 11 Jun 2020

Ito Kentaro, Murayama Yasuto, Kurokawa Yumiko, Kanamaru Shuji, Kokabu Yuichi, Maki Takahisa, Mikawa Tsutomu, Argunhan Bilge, Tsubouchi Hideo, Ikeguchi Mitsunori, Takahashi Masayuki, Iwasaki Hiroshi

Abstract excerpt

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...

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Share to Adenosine Triphosphate
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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: 32528002
DOI: 10.1038/s41467-020-16750-3
PMCID: PMC7289862

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