Swi5-Sfr1 protein stimulates Rad51-mediated DNA strand exchange reaction through organization of DNA bases in the presynaptic filament.
AuthorsFornander, Louise H
KAUST Grant NumberKUK-11-008-23
Permanent link to this recordhttp://hdl.handle.net/10754/596820
MetadataShow full item record
AbstractThe 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.
CitationFornander 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.
SponsorsKing 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].
PublisherOxford University Press (OUP)
JournalNucleic Acids Research
PubMed Central IDPMC3936755
CollectionsPublications Acknowledging KAUST Support
Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution License (), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
- Enhancement of ADP release from the RAD51 presynaptic filament by the SWI5-SFR1 complex.
- Authors: Su GC, Chung CI, Liao CY, Lin SW, Tsai CT, Huang T, Li HW, Chi P
- Issue date: 2014 Jan
- Fission yeast Swi5-Sfr1 protein complex, an activator of Rad51 recombinase, forms an extremely elongated dogleg-shaped structure.
- Authors: Kokabu Y, Murayama Y, Kuwabara N, Oroguchi T, Hashimoto H, Tsutsui Y, Nozaki N, Akashi S, Unzai S, Shimizu T, Iwasaki H, Sato M, Ikeguchi M
- Issue date: 2011 Dec 16
- The Swi5-Sfr1 complex stimulates Rhp51/Rad51- and Dmc1-mediated DNA strand exchange in vitro.
- Authors: Haruta N, Kurokawa Y, Murayama Y, Akamatsu Y, Unzai S, Tsutsui Y, Iwasaki H
- Issue date: 2006 Sep
- Reconstitution of DNA strand exchange mediated by Rhp51 recombinase and two mediators.
- Authors: Kurokawa Y, Murayama Y, Haruta-Takahashi N, Urabe I, Iwasaki H
- Issue date: 2008 Apr 15
- Mechanistic insights into the activation of Rad51-mediated strand exchange from the structure of a recombination activator, the Swi5-Sfr1 complex.
- Authors: Kuwabara N, Murayama Y, Hashimoto H, Kokabu Y, Ikeguchi M, Sato M, Mayanagi K, Tsutsui Y, Iwasaki H, Shimizu T
- Issue date: 2012 Mar 7