Swi5-Sfr1 protein stimulates Rad51-mediated DNA strand exchange reaction through organization of DNA bases in the presynaptic filament.
Type
ArticleAuthors
Fornander, Louise HRenodon-Cornière, Axelle
Kuwabara, Naoyuki
Ito, Kentaro
Tsutsui, Yasuhiro
Shimizu, Toshiyuki
Iwasaki, Hiroshi
Nordén, Bengt
Takahashi, Masayuki
KAUST Grant Number
KUK-11-008-23Date
2013-12-03Online Publication Date
2013-12-03Print Publication Date
2014-02Permanent link to this record
http://hdl.handle.net/10754/596820
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The Swi5-Sfr1 heterodimer protein stimulates the Rad51-promoted DNA strand exchange reaction, a crucial step in homologous recombination. To clarify how this accessory protein acts on the strand exchange reaction, we have analyzed how the structure of the primary reaction intermediate, the Rad51/single-stranded DNA (ssDNA) complex filament formed in the presence of ATP, is affected by Swi5-Sfr1. Using flow linear dichroism spectroscopy, we observe that the nucleobases of the ssDNA are more perpendicularly aligned to the filament axis in the presence of Swi5-Sfr1, whereas the bases are more randomly oriented in the absence of Swi5-Sfr1. When using a modified version of the natural protein where the N-terminal part of Sfr1 is deleted, which has no affinity for DNA but maintained ability to stimulate the strand exchange reaction, we still observe the improved perpendicular DNA base orientation. This indicates that Swi5-Sfr1 exerts its activating effect through interaction with the Rad51 filament mainly and not with the DNA. We propose that the role of a coplanar alignment of nucleobases induced by Swi5-Sfr1 in the presynaptic Rad51/ssDNA complex is to facilitate the critical matching with an invading double-stranded DNA, hence stimulating the strand exchange reaction.Citation
Fornander LH, Renodon-Corniere A, Kuwabara N, Ito K, Tsutsui Y, et al. (2013) Swi5-Sfr1 protein stimulates Rad51-mediated DNA strand exchange reaction through organization of DNA bases in the presynaptic filament. Nucleic Acids Research 42: 2358–2365. Available: http://dx.doi.org/10.1093/nar/gkt1257.Sponsors
King Abdullah University of Science and Technology Grant [KUK-11-008-23 to L.F.]; the Agence Nationale de la Recherche Grant [ANR-2010-BLAN-1013 DynRec to A.R-C. and M.T.]; the European Research Council [ERC-2008-AdG 227700 to B.N.]; Ministry of Education, Culture, Sports, Science and Technology (MEXT) Japan [22125003 to H.I.]; and Japan Society for the Promotion of Science (JSPS) KAKENHI Grant [23770105 to N.K.]; The visit of M.T. to Japan was supported by JSPS Short-term Fellowship and that of N.K. to France by JSPS Institutional Program for Young Researcher Overseas Visits. Funding for open access charge: The Agence Nationale de la Recherche [ANR-2010-BLAN-1013].Publisher
Oxford University Press (OUP)Journal
Nucleic Acids ResearchPubMed ID
24304898PubMed Central ID
PMC3936755ae974a485f413a2113503eed53cd6c53
10.1093/nar/gkt1257
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