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Showing SFR1 — MEI5 is a alias.

SFR1

Swi5-dependent recombination DNA repair protein 1 homolog · UniProt Q86XK3

Length
245 aa
Mass
28.3 kDa
Annotated
2026-06-10
35 papers in source corpus 28 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SFR1 (Sfr1/Mei5) is a conserved auxiliary factor for the eukaryotic RAD51/Dmc1 recombinases that promotes homologous recombination by acting on presynaptic filament dynamics (PMID:20976249, PMID:22492707, PMID:30297419). It functions exclusively as a heterodimer with SWI5 (Sae3), assembling in a 1:1 stoichiometry into an extremely elongated, sharply kinked crescent-shaped molecule—built from a Swi5-Sfr1 parallel coiled-coil core joined by leucine zippers—whose geometry fits the helical groove of the RAD51 filament; the two subunits are mutually interdependent for stability and neither alone substitutes for the complex (PMID:22033972, PMID:22492707, PMID:22405003, PMID:20976249). The complex physically engages RAD51 through the C-terminal domain of SWI5 and through two cooperative binding sites in the intrinsically disordered N-terminus of Sfr1, and this physical interaction is indispensable for stimulating recombinase activity (PMID:27131790, PMID:32204793). Mechanistically, SWI5-SFR1 stabilizes the RAD51-ssDNA presynaptic filament by reducing RAD51 dissociation, lowering the effective nucleation size, and shifting RAD51 oligomerization toward smaller units to favor uniform filament extension (PMID:30297419, PMID:40682818); it maintains the catalytically active ATP-bound filament state by facilitating ADP release rather than by blocking ATP hydrolysis (PMID:24078249, PMID:41206037), and it functions as a direct activator of RAD51 strand exchange by driving the C1→C2 transition and releasing ssDNA (PMID:39340300). In meiosis the complex serves a dual role with the Dmc1 recombinase—loading Dmc1 onto RPA-coated ssDNA as a mediator and stabilizing nucleating Dmc1 clusters to promote RPA displacement (PMID:24186976, PMID:39275989, PMID:39340300)—and its activity is downregulated by CDK phosphorylation of the Sfr1 disordered N-terminus during late meiotic prophase, which inhibits RAD51 binding and chromosome loading to ensure timely resolution of recombination intermediates (PMID:37330173, PMID:39174851). Loss of SWI5 or SFR1 sensitizes cells to ionizing radiation, camptothecin, and PARP inhibition with attenuated sister chromatid exchange and increased chromosome aberrations (PMID:20976249). Human SFR1 additionally interacts with estrogen receptor alpha and potentiates its transcriptional activity (PMID:23874500).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2004 High

    Established that the Mei5-Sae3 (SFR1-SWI5) complex is a dedicated loading factor for the meiotic recombinase Dmc1, defining its first cellular function as distinct from the generic Rad51 pathway.

    Evidence Genetic epistasis, co-IP, and chromosome immunofluorescence in budding yeast meiosis

    PMID:15579681 PMID:15620352

    Open questions at the time
    • Did not establish the biochemical mechanism of Dmc1 loading
    • Mitotic/Rad51-directed role not addressed
  2. 2006 High

    Showed the complex acts catalytically (substoichiometric) in vitro to overcome RPA inhibition of strand exchange, framing it as a recombination accessory factor for both Rad51 and Dmc1.

    Evidence In vitro strand exchange and ATPase assays with purified fission yeast proteins

    PMID:16921379

    Open questions at the time
    • Did not resolve whether stimulation acts on filament assembly versus catalysis
    • No structural basis for RAD51 engagement
  3. 2007 High

    Placed Swi5-Sfr1 in a distinct HR sub-branch from Rhp55/57 in cells, showing partially redundant but mechanistically separate mediator roles.

    Evidence Live microscopy of damage-induced foci and genetic epistasis with double mutants in fission yeast

    PMID:17304215

    Open questions at the time
    • Molecular basis for branch distinction not defined
    • Crossover-specific roles not assigned to the complex
  4. 2009 High

    Demonstrated direct biochemical mediator activity: Mei5-Sae3 binds ssDNA, interacts with RPA, and relieves RPA inhibition of Dmc1, providing a mechanism for the genetic loading phenotype.

    Evidence In vitro strand assimilation, DNA binding, and RPA co-IP with purified budding yeast proteins

    PMID:19270307

    Open questions at the time
    • Did not visualize the RPA-to-Dmc1 handoff intermediate
    • Stoichiometry of the active species unresolved
  5. 2011 High

    Defined the solution architecture as a 1:1 elongated dogleg heterodimer suited to fit the Rad51 filament groove, linking shape to function.

    Evidence SAXS, analytical ultracentrifugation, mass spectrometry, and Fab topology mapping; species comparison resolving DNA-binding versus stabilization roles

    PMID:21543267 PMID:22033972

    Open questions at the time
    • No atomic-resolution structure yet
    • Filament-groove docking inferred, not directly observed
  6. 2012 High

    Extended the mechanism to mammals and provided atomic detail: the heterodimer stabilizes the Rad51 presynaptic filament and adopts a kinked crescent core via leucine-zipper-joined coiled coils, with the Sfr1 N-terminus providing the Rad51 interface.

    Evidence In vitro DNA pairing and filament stability assays with mouse proteins plus 2.3 Å crystal structure of the fission yeast core domain

    PMID:22405003 PMID:22492707

    Open questions at the time
    • N-terminal disordered region not resolved crystallographically
    • RSfp regulatory motif mechanism in mammals undefined
  7. 2013 High

    Resolved the catalytic mechanism of filament stabilization as ADP release maintaining the active ATP-bound state, and distinguished mediator (Dmc1) from activator roles, while also revealing a non-recombination role in ERα transcription.

    Evidence Optical tweezers single-molecule and ensemble ATPase assays; flow linear dichroism; competitive strand exchange with Rad22; and Y2H/Co-IP/ChIP for human SFR1-ERα

    PMID:23828040 PMID:23874500 PMID:24078249 PMID:24186976 PMID:24304898

    Open questions at the time
    • ERα transcriptional role (Medium) characterized in a single lab without reciprocal validation
    • Physiological significance of the transcriptional role versus recombination role unresolved
  8. 2016 High

    Established that direct physical contact via the SWI5 C-terminus is indispensable for functional stimulation, ruling out an indirect or DNA-only mechanism.

    Evidence Interaction-defective domain/point mutants combined with in vitro strand exchange and AUC of mouse proteins

    PMID:27131790

    Open questions at the time
    • Did not map the reciprocal RAD51 interface
    • Trimeric complex geometry not determined structurally
  9. 2018 High

    Quantified the conserved kinetic mechanism: the complex reduces RAD51 nucleation size and dissociation, stabilizing filaments across mouse and fission yeast.

    Evidence Single-molecule TPM and smFRET with two-species comparison

    PMID:30297419

    Open questions at the time
    • Did not address oligomeric state changes during extension
    • Meiotic Dmc1 kinetics not measured in the same framework
  10. 2019 Medium

    Showed in vivo that Mei5-Sae3 limits Dmc1 filament length to prevent aberrant recombination, linking filament regulation to genome stability.

    Evidence Gain-of-function dmc1-E157D genetics, double mutants, and STORM super-resolution imaging in budding yeast

    PMID:31790385

    Open questions at the time
    • Mechanism of length limitation not biochemically reconstituted
    • Single-lab genetic analysis
  11. 2020 High

    Mapped two cooperative Rad51-binding sites in the intrinsically disordered Sfr1 N-terminus and showed the complex can cooperate with Rad55-Rad57 in a higher-order assembly.

    Evidence NMR, biochemical binding/stimulation assays, yeast sensitivity assays, and Co-IP in fission yeast

    PMID:32204793

    Open questions at the time
    • Architecture of the Swi5-Sfr1/Rad55-Rad57 super-complex undefined
    • Whether mammalian SFR1 has the same dual sites untested here
  12. 2021 Medium

    Identified meiotic phosphorylation of Swi5 and Sfr1, with phosphomimetic mutants partially impairing function, opening a regulatory dimension to complex activity.

    Evidence Mass spectrometry of complex from meiotic cells plus phosphomimetic/phospho-blocking mutagenesis with functional assays

    PMID:34208949

    Open questions at the time
    • Writer kinase not identified at this stage
    • Full mechanistic significance left unresolved by authors
  13. 2023 High

    Linked phosphorylation of the Sfr1 disordered domain directly to regulated Rad51 binding, showing reversible (not merely added) phosphorylation tunes the interaction.

    Evidence Biochemical reconstitution with phosphomimetic/phospho-blocking mutants, binding and strand exchange assays, and yeast damage sensitivity

    PMID:37330173

    Open questions at the time
    • Identity of the kinase inferred from motifs, not proven
    • Dephosphorylation/phosphatase not addressed
  14. 2024 High

    Defined the meiotic regulatory circuit: CDK phosphorylates the Sfr1 N-terminal disordered platform during prophase to downregulate Rad51 binding/loading and tune interhomolog recombination timing, with separable activator (Rad51) versus mediator (Dmc1) mechanisms and meiosis-specific Mei5 processing.

    Evidence sfr1-7D/7A genetic mutants with chromosome immunofluorescence and cytology; real-time strand exchange kinetics (C1/C2 intermediates); smFRET/CoSMoS RPA-displacement assays; Mei5 basic-residue mutagenesis with Co-IP

    PMID:38924305 PMID:39174851 PMID:39275989 PMID:39340300

    Open questions at the time
    • Whether CDK regulation is conserved in mammalian SFR1 untested
    • Meiosis-specific Mei5 truncation (Medium) and its protease not defined
  15. 2025 High

    Refined the filament mechanism by showing the complex modulates RAD51 oligomeric state (octamer→tetramer) in solution to promote uniform extension, and demonstrated that stabilization of the active Dmc1/Rad51 filament is independent of altering the ATP hydrolytic cycle.

    Evidence Single-molecule TPM step-size analysis with mouse proteins; in vitro filament stability and ATPase assays with nucleotide and E157D comparisons in budding yeast

    PMID:40682818 PMID:41206037

    Open questions at the time
    • Step-size/oligomer model (Medium) rests on a single method without orthogonal validation
    • Structural basis for oligomer modulation unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether the meiotic CDK-phosphorylation regulatory mechanism and the human ERα transcriptional role of SFR1 are conserved and functionally integrated with its recombination function in mammals remains unresolved.
  • No mammalian in vivo test of CDK regulation of SFR1
  • Relationship between SFR1's transcriptional and recombination roles uncharacterized
  • No atomic structure of the trimeric RAD51-SWI5-SFR1 complex

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 6 GO:0060090 molecular adaptor activity 3 GO:0003677 DNA binding 2 GO:0140110 transcription regulator activity 1
Localization
GO:0005634 nucleus 3 GO:0005694 chromosome 2
Pathway
R-HSA-1474165 Reproduction 3 R-HSA-73894 DNA Repair 2 R-HSA-74160 Gene expression (Transcription) 1
Partners
DMC1ESR1RAD51RAD55RAD57RPASWI5
Complex memberships
RAD51-SWI5-SFR1 trimeric complexSWI5-SFR1 (Mei5-Sae3) heterodimerSwi5-Sfr1/Rad55-Rad57 higher-order complex

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 Yeast Mei5 and Sae3 (orthologs of human SFR1/SWI5) form a ternary complex with Dmc1 and are required for assembly of Dmc1 (but not Rad51) onto chromosomes, acting as loading factors for the Dmc1 recombinase; their chromosome association requires Rad51, and they are mutually dependent with Dmc1 for localization. Genetic epistasis (sporulation, spore viability, crossing-over assays in mei5, sae3, dmc1 mutants), co-immunoprecipitation, chromatin immunofluorescence, recombination hot-spot ChIP Cell High 15579681 15620352
2006 The S. pombe Swi5-Sfr1 complex (ortholog of human SWI5-SFR1) stimulates Rad51 (Rhp51)- and Dmc1-mediated DNA strand exchange in vitro at substoichiometric concentrations by overcoming RPA inhibition; it preferentially stimulates the ssDNA-dependent ATPase activity of Rhp51 and increases the amount of Dmc1 bound to ssDNA. In vitro strand exchange assay, ssDNA-dependent ATPase assay, DNA binding assay with purified recombinant proteins Nature structural & molecular biology High 16921379
2007 In fission yeast, Swi5 localizes to the nucleus forming diffuse staining with foci; upon UV irradiation, Sfr1 forms foci colocalizing with damage-induced Rhp51 foci. Swi5/Sfr1 acts as a Rad51 mediator but processes DSBs differently from Rhp55/57: swi5Δ rhp57Δ double mutant completely abolishes UV-induced Rhp51 foci, while Rhp51 and Rhp57 (not Swi5/Sfr1) are essential for crossover production. Live fluorescence microscopy (GFP fusions), UV irradiation assays, HO endonuclease-induced DSB assay, genetic epistasis with double mutants The EMBO journal High 17304215
2009 S. cerevisiae Mei5-Sae3 complex preferentially binds single-stranded DNA, physically interacts with RPA, and relieves RPA-mediated inhibition of Dmc1 strand assimilation and DNA binding, functioning as a recombination mediator for Dmc1 assembly. In vitro strand assimilation assay, DNA binding assays, co-immunoprecipitation with RPA, purified recombinant protein biochemistry The Journal of biological chemistry High 19270307
2010 Mammalian Swi5 and Sfr1 are nuclear proteins that form a heterodimeric complex in vivo and in vitro; Swi5 interacts in vitro with Rad51. Both proteins are mutually interdependent for stability. The complex is required for HR when Rad51 is perturbed by a BRC peptide; Swi5−/− and Sfr1−/− ES cells are sensitive to ionizing radiation, camptothecin, and PARP inhibitor olaparib, show attenuated sister chromatid exchange, and increased chromosome aberrations. Co-immunoprecipitation (in vivo and in vitro), nuclear localization by microscopy, genetic knockout of mouse Swi5 and Sfr1 in ES cells, clonogenic survival assays, sister chromatid exchange assay, chromosome aberration analysis PLoS genetics High 20976249
2011 The fission yeast Swi5-Sfr1 complex exists in a 1:1 stoichiometry (heterodimer) and adopts an extremely elongated dogleg-shaped structure in solution (high frictional ratio f/f0 = 2.0), as determined by SAXS and analytical ultracentrifugation; topology mapping with Fab fragments suggests the complex fits into the groove of the Rad51 filament. Small-angle X-ray scattering (SAXS), analytical ultracentrifugation, electrospray ionization mass spectrometry, Fab-fragment topology mapping The Journal of biological chemistry High 22033972
2011 The budding yeast Mei5-Sae3 complex preferentially binds fork-like DNA substrates over 3'-overhang, ssDNA, or dsDNA; DNA binding activity is conferred by the Mei5 subunit. Mei5-Sae3 interacts with Rad51 through the N-terminal domain of Mei5. Unlike Rad52, Mei5-Sae3 lacks recombination mediator activity for Rad51 and lacks ssDNA annealing activity. Electrophoretic mobility shift assay (EMSA) with purified proteins, DNA substrate binding assays, co-immunoprecipitation/pulldown with Rad51 DNA repair Medium 21543267
2012 Mouse Swi5-Sfr1 heterodimer (1:1 stoichiometry) physically interacts with Rad51 and stabilizes the Rad51-ssDNA presynaptic filament, stimulating homologous DNA pairing; neither Swi5 nor Sfr1 alone can substitute for the complex. The RSfp (rodent Sfr1 proline-rich) motif in Sfr1 acts as a negative regulatory element. Biophysical characterization (analytical ultracentrifugation), in vitro Rad51-mediated DNA pairing assay, presynaptic filament stability assay, domain mutagenesis (RSfp deletion) Nucleic acids research High 22492707
2012 Crystal structure of the fission yeast Swi5-Sfr1 complex (C-terminal core domain of Sfr1 with Swi5) reveals a parallel coiled-coil heterodimer joined by two leucine-zipper motifs and a bundle, forming a sharply kinked elongated crescent shape suited for binding within the helical groove of the Rad51 filament; the N-terminal region of Sfr1 provides a Rad51-binding interface. X-ray crystallography (2.3 Å resolution), mutagenesis-guided functional validation Structure High 22405003
2013 SWI5-SFR1 facilitates ADP release from the RAD51 presynaptic filament, thereby maintaining the ATP-bound (catalytically active) state of the filament; this is distinct from simply blocking ATP hydrolysis. SWI5-SFR1 also enhances ATP hydrolysis by ssDNA-bound RAD51. Optical tweezers single-molecule experiments, biochemical ATPase assays, ADP release kinetics with purified proteins Nucleic acids research High 24078249
2013 Swi5-Sfr1 promotes more perpendicular alignment of nucleobases (coplanar alignment) in the Rad51/ssDNA presynaptic filament, as measured by flow linear dichroism spectroscopy; this structural change is mediated through interaction with the Rad51 filament rather than directly with DNA, as a ΔN-Sfr1 mutant lacking DNA affinity still induces the same base orientation change. Flow linear dichroism spectroscopy, N-terminal deletion mutant of Sfr1 Nucleic acids research Medium 24304898
2013 In fission yeast, Swi5-Sfr1 is a mediator that loads Dmc1 onto RPA-coated ssDNA and a direct activator of Dmc1 strand exchange; in contrast, Rad22 (fission yeast Rad52) inhibits Dmc1 by competing for binding to RPA-coated ssDNA, while activating Rad51. In vitro strand exchange assay with purified Dmc1, Swi5-Sfr1, Rad22, and RPA; competitive binding assays Genes & development High 24186976
2013 Human SFR1 physically interacts with estrogen receptor alpha (ERα): interaction initially identified by yeast two-hybrid and confirmed by co-immunoprecipitation in mammalian cells. SFR1 co-localizes with ERα in the nucleus, potentiates ERα transcriptional activity (ligand-dependent and -independent), occupies ER-target gene promoters by ChIP, and SFR1 knockdown diminishes ER transcriptional activity. Yeast two-hybrid screen, co-immunoprecipitation, mammalian one-hybrid assay, co-localization by microscopy, ChIP, siRNA knockdown PloS one Medium 23874500
2013 In fission yeast, Rrp1 and Rrp2 interact with Swi5 (two-hybrid), form co-localizing MMS-induced nuclear foci, and function epistatically with Swi5 and Srs2 (but independently of Rad57), placing them in the Swi5/Sfr1-dependent branch of HR. Yeast two-hybrid, fluorescence microscopy (co-localizing foci), genetic epistasis analysis Nucleic acids research Medium 23828040
2016 The C-terminal domain of mouse SWI5 is required for physical interaction with RAD51; SWI5-SFR1 preferentially associates with oligomeric RAD51. RAD51 interaction-defective mutants of SWI5-SFR1 abolish stimulation of RAD51 recombinase activity, establishing that physical interaction is indispensable for functional stimulation (trimeric RAD51-SWI5-SFR1 complex). Pull-down/co-immunoprecipitation with domain deletion and point mutants, in vitro Rad51 strand exchange assay, analytical ultracentrifugation Nucleic acids research High 27131790
2018 Mouse Swi5-Sfr1 (mS5S1) stimulates Rad51 filament assembly by reducing RAD51 dissociation from filaments, reducing the effective nucleation size from 3 to 2 RAD51 molecules; fission yeast Swi5-Sfr1 similarly reduces SpRad51 disassembly rate to maintain stable filaments, demonstrating a conserved mechanism. Single-molecule tethered particle motion (TPM), single-molecule FRET (smFRET), mouse and fission yeast Rad51 with purified Swi5-Sfr1 Proceedings of the National Academy of Sciences of the United States of America High 30297419
2019 In S. cerevisiae, Mei5-Sae3 (ortholog of SFR1-SWI5) has independent roles: Rad51 function as an accessory factor for Dmc1 filament stability, while the partner Rad51 also functions independently in promoting filament stability. A gain-of-function dmc1-E157D mutant bypasses the requirement for Mei5-Sae3, forms longer filaments prone to aberrant recombination. Mei5-Sae3 limits filament length to prevent genome rearrangements. Genetic analysis (gain-of-function mutant, double mutants), super-resolution microscopy (STORM), analysis of recombination intermediates PLoS genetics Medium 31790385
2020 Two distinct sites within the intrinsically disordered N-terminus of Sfr1 (Sfr1N) cooperatively bind Rad51; deletion of this domain impairs Rad51 stimulation in vitro and causes DNA damage sensitivity in cells. Swi5-Sfr1 and Rad55-Rad57 can form a higher-order complex and collaboratively stimulate Rad51 in S. pombe. NMR, biochemical binding assays (purified proteins), in vitro Rad51 stimulation assays, yeast genetic sensitivity assays, co-immunoprecipitation (higher-order complex) eLife High 32204793
2021 Fission yeast Swi5 and Sfr1 are phosphorylated during meiosis at specific sites identified by mass spectrometry. Phosphomimetic mutations at these sites render Swi5-Sfr1 only partially functional; phospho-blocking mutations do not impair function. Mass spectrometry of purified complex from meiotic cells, mutagenesis (phosphomimetic and phospho-blocking mutants), functional assays in yeast Genes Medium 34208949
2023 Phosphorylation of five residues within the intrinsically disordered domain of fission yeast Sfr1 (by an unspecified kinase, likely CDK based on motifs) regulates its interaction with Rad51; a phosphomimetic Swi5-Sfr1 mutant is defective in both physical and functional interaction with Rad51, resulting in DNA repair deficiency. A phospho-blocking mutant also shows DNA damage sensitivity, indicating that regulated (reversible) phosphorylation is required. Biochemical reconstitution with phosphomimetic/phospho-blocking mutants, in vitro binding and strand exchange assays, yeast genetic DNA damage sensitivity assays The Journal of biological chemistry High 37330173
2023 Swi5-Sfr1 and Hop2-Mnd1 stimulate Dmc1 filament assembly by distinct mechanisms: Hop2-Mnd1 enhances the Dmc1 binding rate (nucleation), while Swi5-Sfr1 specifically reduces the Dmc1 dissociation rate during nucleation (~2-fold); the two complexes act additively when combined. Single-molecule FRET (smFRET), tethered particle motion (TPM), order-of-addition experiments with purified proteins Nucleic acids research High 37395447
2024 CDK phosphorylates fission yeast Sfr1 at multiple sites in its N-terminal disordered domain during meiotic prophase; phospho-mimetic sfr1-7D inhibits Rad51 binding and chromosome loading, decreasing interhomolog recombination. Non-phosphorylatable sfr1-7A alters Rad51 dynamics at late prophase and exacerbates chromatin segregation defects when combined with dbl2 deletion. The N-terminal disordered domain of Sfr1 serves as a CDK-regulated platform. Genetic mutant analysis (phosphomimetic sfr1-7D and non-phosphorylatable sfr1-7A), chromosome immunofluorescence (Rad51 loading), cytology (chromosome segregation), biochemical validation The EMBO journal High 39174851
2024 Mei5-Sae3 stabilizes Dmc1 nucleating clusters (2–3 molecules) on naked ssDNA by preferentially reducing Dmc1 dissociation rates, and also stimulates Dmc1 assembly on RPA-coated ssDNA; an intermediate with coexisting Dmc1 and RPA on ssDNA was observed before RPA dissociation, suggesting Mei5-Sae3 mediates Dmc1 binding by stabilizing nucleating clusters to promote RPA displacement. Single-molecule FRET (smFRET), colocalization single-molecule spectroscopy (CoSMoS), GFP-labeled RPA displacement assay, purified recombinant proteins Nucleic acids research High 39275989
2024 Arg97 of Mei5 (conserved in human SFR1) is critical for complex formation with Sae3 and for Dmc1 assembly; substitution of Arg117 or Lys133 leads to production of a C-terminally truncated Mei5 protein specifically during meiosis (not mitosis), suggesting posttranslational processing unique to meiotic regulation of Dmc1-mediated recombination. Site-directed mutagenesis of Mei5 basic residues, co-immunoprecipitation (complex formation), Western blot (truncated protein), yeast meiosis vs. mitosis comparison Genes to cells Medium 38924305
2024 Swi5-Sfr1 regulates Dmc1- and Rad51-driven strand exchange via distinct mechanisms: for Rad51, it facilitates the C1→C2 transition in strand exchange and releases ssDNA from C2 (activator role); for Dmc1, it enhances association with ssDNA by promoting filament nucleus formation (mediator role), unlike its activator role with Rad51. Real-time in vitro strand exchange assay with fission yeast Dmc1 and Rad51, kinetic analysis of three-stranded intermediates (C1, C2), purified recombinant proteins Nucleic acids research High 39340300
2025 Mouse SWI5-SFR1 reduces the dissociation probability of RAD51 during filament extension, promoting more uniform filament growth; step-size analysis shows RAD51 assembles predominantly as octamers, and in the presence of SWI5-SFR1 the distribution shifts toward tetramers, indicating SWI5-SFR1 modulates the oligomeric state of RAD51 in solution to facilitate extension and stabilize DNA binding. Single-molecule tethered particle motion (TPM) with step-size analysis, purified mouse RAD51 and SWI5-SFR1 Nucleic acids research Medium 40682818
2025 Budding yeast Mei5-Sae3 stabilizes Dmc1 filaments in both active (ATP-bound) and inactive (ADP-bound) conformations; it specifically stabilizes the active filament form without inhibiting ATP hydrolysis—indeed it increases ATP hydrolysis—unlike calcium, AMP-PNP, or the E157D mutation which stabilize filaments by blocking hydrolysis. This demonstrates Mei5-Sae3's filament stabilization does not depend on alteration of the hydrolytic cycle. In vitro filament stability assays, ATPase assays, nucleotide cofactor substitution experiments, dmc1-E157D gain-of-function comparison, purified recombinant proteins Nucleic acids research High 41206037

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 A protein complex containing Mei5 and Sae3 promotes the assembly of the meiosis-specific RecA homolog Dmc1. Cell 113 15620352
2006 The Swi5-Sfr1 complex stimulates Rhp51/Rad51- and Dmc1-mediated DNA strand exchange in vitro. Nature structural & molecular biology 104 16921379
2004 The budding yeast mei5 and sae3 proteins act together with dmc1 during meiotic recombination. Genetics 77 15579681
2007 Fission yeast Swi5/Sfr1 and Rhp55/Rhp57 differentially regulate Rhp51-dependent recombination outcomes. The EMBO journal 69 17304215
2009 The Mei5-Sae3 protein complex mediates Dmc1 activity in Saccharomyces cerevisiae. The Journal of biological chemistry 47 19270307
2010 Role for the mammalian Swi5-Sfr1 complex in DNA strand break repair through homologous recombination. PLoS genetics 45 20976249
2012 Mechanistic insights into the activation of Rad51-mediated strand exchange from the structure of a recombination activator, the Swi5-Sfr1 complex. Structure (London, England : 1993) 37 22405003
2012 Rad51 presynaptic filament stabilization function of the mouse Swi5-Sfr1 heterodimeric complex. Nucleic acids research 37 22492707
2013 Characterisation of an intrinsically disordered protein complex of Swi5-Sfr1 by ion mobility mass spectrometry and small-angle X-ray scattering. The Analyst 31 23324799
2013 Enhancement of ADP release from the RAD51 presynaptic filament by the SWI5-SFR1 complex. Nucleic acids research 28 24078249
2018 Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation. Proceedings of the National Academy of Sciences of the United States of America 27 30297419
2011 Fission yeast Swi5-Sfr1 protein complex, an activator of Rad51 recombinase, forms an extremely elongated dogleg-shaped structure. The Journal of biological chemistry 25 22033972
2011 The budding yeast Mei5-Sae3 complex interacts with Rad51 and preferentially binds a DNA fork structure. DNA repair 24 21543267
2017 The differentiated and conserved roles of Swi5-Sfr1 in homologous recombination. FEBS letters 23 28423184
2016 Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination. Nucleic acids research 16 27131790
2013 Dual regulation of Dmc1-driven DNA strand exchange by Swi5-Sfr1 activation and Rad22 inhibition. Genes & development 15 24186976
2013 Swi5-Sfr1 protein stimulates Rad51-mediated DNA strand exchange reaction through organization of DNA bases in the presynaptic filament. Nucleic acids research 15 24304898
2019 A mutant form of Dmc1 that bypasses the requirement for accessory protein Mei5-Sae3 reveals independent activities of Mei5-Sae3 and Rad51 in Dmc1 filament stability. PLoS genetics 12 31790385
2020 Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex. eLife 10 32204793
2008 Genetic analysis reveals different roles of Schizosaccharomyces pombe sfr1/dds20 in meiotic and mitotic DNA recombination and repair. Current genetics 10 18769921
2023 Hop2-Mnd1 and Swi5-Sfr1 stimulate Dmc1 filament assembly using distinct mechanisms. Nucleic acids research 8 37395447
2013 Involvement of Schizosaccharomyces pombe rrp1+ and rrp2+ in the Srs2- and Swi5/Sfr1-dependent pathway in response to DNA damage and replication inhibition. Nucleic acids research 8 23828040
2010 Expression, purification and crystallization of Swi5 and the Swi5-Sfr1 complex from fission yeast. Acta crystallographica. Section F, Structural biology and crystallization communications 7 20823543
2013 DNA homologous recombination factor SFR1 physically and functionally interacts with estrogen receptor alpha. PloS one 5 23874500
2021 Mapping and Analysis of Swi5 and Sfr1 Phosphorylation Sites. Genes 4 34208949
2016 Sfr1, a Tetrahymena thermophila Sfi1 Repeat Protein, Modulates the Production of Cortical Row Basal Bodies. mSphere 4 27904881
2024 Mei5-Sae3 stabilizes Dmc1 nucleating clusters for efficient Dmc1 assembly on RPA-coated single-stranded DNA. Nucleic acids research 3 39275989
2023 Phosphoregulation of DNA repair via the Rad51 auxiliary factor Swi5-Sfr1. The Journal of biological chemistry 3 37330173
2024 Mutational analysis of Mei5, a subunit of Mei5-Sae3 complex, in Dmc1-mediated recombination during yeast meiosis. Genes to cells : devoted to molecular & cellular mechanisms 2 38924305
2024 CDK phosphorylation of Sfr1 downregulates Rad51 function in late-meiotic homolog invasions. The EMBO journal 2 39174851
2023 The role of conserved amino acid residues of Sae3 in Mei5-Sae3 complex for Dmc1 assembly in meiotic recombination. Genes & genetic systems 2 37225456
2024 Genomic Sequence of Streptococcus salivarius MDI13 and Latilactobacillus sakei MEI5: Two Promising Probiotic Strains Isolated from European Hakes (Merluccius merluccius, L.). Veterinary sciences 1 39195819
2024 The Swi5-Sfr1 complex regulates Dmc1- and Rad51-driven DNA strand exchange proceeding through two distinct three-stranded intermediates by different mechanisms. Nucleic acids research 1 39340300
2025 SWI5-SFR1 reduces RAD51 recombinase extending units during filament assembly. Nucleic acids research 0 40682818
2025 Mei5-Sae3 stabilizes both active and inactive forms of Dmc1 filaments independently of its impact on ATP hydrolysis. Nucleic acids research 0 41206037

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