Affinage

DMC1

Protein HID1 · UniProt Q8IV36

Length
788 aa
Mass
88.7 kDa
Annotated
2026-06-09
100 papers in source corpus 51 papers cited in narrative 50 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DMC1 is a meiosis-specific RecA/RAD51-family recombinase that catalyzes the homologous strand-exchange reaction underlying meiotic recombination, and its loss arrests cells in meiotic prophase with unrepaired double-strand-break intermediates and failed homolog synapsis (PMID:1581960, PMID:9660953, PMID:9660954). Mechanistically, DMC1 assembles on resected single-stranded DNA at programmed DSBs—in mammalian meiosis it binds near the break end while RAD51 occupies positions away from the break, identifying DMC1 as the principal strand-exchange enzyme in vivo (PMID:32610038). Purified DMC1 binds ssDNA and dsDNA, possesses weak DNA-dependent ATPase activity, and performs ATP-dependent strand exchange and D-loop formation through a presynaptic nucleoprotein filament; ATP binding rather than hydrolysis supports the active filament, and Ca2+ stabilizes it (PMID:11551925, PMID:15164066, PMID:15917244, PMID:16204247). Although human DMC1 can be captured as an octameric ring stabilized by an N-terminal-domain interface absent in RAD51, the functional filament is helical and structurally near-identical to RAD51, so its distinctive meiotic behavior arises from sequence-specific features and accessory factors rather than gross filament architecture (PMID:10485886, PMID:15125839, PMID:15917243, PMID:18535008). A defining property is mismatch tolerance during strand exchange, conferred by DMC1-specific Loop1/Loop2 residues (Gln244, Pro274/Gly275) that form an open 'triplet gate' permitting heteroduplex with mismatches; transplanting these residues between DMC1 and RAD51 swaps their fidelity (PMID:31371435, PMID:34871438, PMID:33446654). DMC1-generated D-loops are intrinsically resistant to branch-migration dissociation and DMC1 inhibits the Srs2 anti-recombinase, properties that protect joint molecules and channel intermediates toward crossover formation (PMID:21151113, PMID:30301803). DMC1 activity is governed by a network of accessory factors: HOP2-MND1 stimulates pairing by stabilizing the presynaptic filament and promoting duplex capture, Mei5-Sae3 and Swi5-Sfr1 relieve RPA inhibition and mediate filament assembly, BRCA2 and RAD51AP1 act as mediators via DMC1-specific motifs (the BRCA2 PhePP and RAD51AP1 WVPP motifs), Tid1/Rdh54 enhances joint-molecule formation while clearing DMC1 from nonproductive chromatin, and FIGNL1 dismantles DMC1 filaments (PMID:15249670, PMID:15834424, PMID:15579681, PMID:19270307, PMID:16921379, PMID:17541404, PMID:21307306, PMID:26976601, PMID:22761450, PMID:16980587, PMID:37891173). RAD51 itself functions partly as a DMC1 accessory factor whose joint-molecule activity is dispensable for meiotic recombination, since DMC1's strand-exchange activity alone drives the process (PMID:22955832).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 1992 High

    Established that meiotic recombination requires a dedicated, meiosis-specific RecA-like enzyme, defining DMC1 as a core factor whose absence blocks reciprocal recombination and prophase progression.

    Evidence Genetic loss-of-function and mutant phenotyping in budding yeast

    PMID:1581960

    Open questions at the time
    • No biochemical activity demonstrated
    • Relationship to RAD51 unresolved
  2. 1994 High

    Placed DMC1 in an ordered relationship with RAD51 at recombination sites by showing DMC1 focus formation depends on RAD51, framing the two recombinases as cooperating but distinct.

    Evidence Immunostaining of spread meiotic nuclei with rad51/dmc1/zip1 epistasis

    PMID:7528104

    Open questions at the time
    • Molecular basis of co-dependence unknown
    • Whether colocalization reflects mixed filaments untested
  3. 1998 High

    Demonstrated DMC1 is essential for homolog synapsis and fertility in a mammal, establishing conservation of its meiotic role and showing axial elements form without DMC1 but pairing fails.

    Evidence Dmc1-null knockout mice, cytology of spermatocytes/oocytes

    PMID:9660953 PMID:9660954

    Open questions at the time
    • Catalytic mechanism in vivo not addressed
    • Sex differences not yet dissected
  4. 2004 High

    Reconstituted DMC1 as a bona fide ATP-dependent strand-exchange recombinase that nucleates a helical filament on ssDNA and requires RPA, defining its core enzymatic activity.

    Evidence In vitro strand exchange and EM with purified human protein; earlier yeast strand-assimilation biochemistry

    PMID:11551925 PMID:15164066

    Open questions at the time
    • In vivo filament composition not addressed
    • Crossover-bias mechanism unknown
  5. 2004 High

    Resolved the structural paradox between DMC1's octameric ring and active filament by crystallizing the human octamer, mapping DNA-binding patches, and tracing ring stabilization to an N-terminal interface absent in RAD51.

    Evidence X-ray crystallography, mutagenesis, DNA-binding and oligomerization assays

    PMID:15125839 PMID:15917243 PMID:15917244

    Open questions at the time
    • Functional role of octamer vs filament unresolved
    • Crystal lacked DNA-bound filament
  6. 2005 High

    Identified Mei5-Sae3 and HOP2-MND1 as mediators that overcome RPA inhibition and stimulate DMC1 filament assembly and pairing, explaining how DMC1 is loaded and activated at DSBs.

    Evidence In vitro reconstitution, DNA-binding, ChIP, cytology and genetics across yeast and mouse orthologs

    PMID:15192114 PMID:15249670 PMID:15579681 PMID:15620352 PMID:15834424 PMID:19270307

    Open questions at the time
    • Stoichiometry on chromatin in vivo unclear
    • Order of mediator action incompletely defined
  7. 2006 High

    Defined Tid1/Rdh54 and Rad54B as DMC1 partners that both stimulate recombinase activity and clear DMC1 from nonproductive chromatin, introducing quality-control of filament placement.

    Evidence ChIP and genetics; in vitro recombinase, dsDNA-dissociation and ATPase-mutant assays

    PMID:16921379 PMID:16945962 PMID:16980587 PMID:19028606

    Open questions at the time
    • How removal is targeted to nonproductive sites mechanistically incomplete
  8. 2007 High

    Mapped a dedicated DMC1-binding site on BRCA2 (the PhePP motif), distinct from its RAD51 site, and a defective L2 DNA-binding allele in mouse, linking specific DMC1 contacts and residues to meiotic strand-invasion function.

    Evidence BRCA2 truncation/point-mutant binding assays; mouse Dmc1Mei11 mutant with in vitro activity loss and cytology

    PMID:17425408 PMID:17541404

    Open questions at the time
    • In vivo consequence of BRCA2-DMC1 disruption alone not isolated
    • Basis of sex-specific dependence unexplained
  9. 2010 High

    Provided a mechanistic basis for DMC1's pro-crossover function by showing its D-loops resist branch-migration dissociation far better than RAD51 D-loops.

    Evidence In vitro D-loop formation/dissociation with purified human DMC1, RAD51, RAD54

    PMID:21151113

    Open questions at the time
    • Direct link to crossover vs non-crossover choice in vivo not shown
  10. 2011 High

    Established RAD51AP1 as a DMC1 mediator acting through a conserved WVPP motif that enhances duplex capture, paralleling the BRCA2 PhePP motif and revealing a shared interaction logic among DMC1 mediators.

    Evidence Co-IP, motif mutagenesis, in vitro D-loop/synaptic complex assays, mouse spermatocyte colocalization

    PMID:21307306 PMID:21903585

    Open questions at the time
    • In vivo requirement for the WVPP-DMC1 contact during meiosis untested
  11. 2012 High

    Separated the meiotic roles of the two recombinases, showing DMC1's joint-molecule activity drives meiotic recombination while RAD51 functions as a DMC1 accessory whose own JM activity is dispensable.

    Evidence Separation-of-function alleles in yeast plus in vitro biochemistry; DMC1-Tid1 vs RAD51-Rad54 pairing specificity

    PMID:22761450 PMID:22955832

    Open questions at the time
    • Molecular basis of interhomolog bias incompletely defined
  12. 2016 High

    Showed full-length BRCA2 acts as a genuine DMC1 mediator and defined BRC-repeat specialization, with BRC repeats 6-8 binding DMC1 preferentially and stimulating filament formation and strand exchange.

    Evidence In vitro reconstitution with purified full-length BRCA2 and BRC-repeat panel

    PMID:26976601

    Open questions at the time
    • Coordination of BRCA2 between RAD51 and DMC1 in cells not resolved
  13. 2019 High

    Pinpointed the molecular origin of DMC1's hallmark mismatch tolerance to a small set of DMC1-specific residues, since transplanting them confers tolerance on RAD51 and removing them abolishes it.

    Evidence Chimeric mutagenesis, in vitro strand exchange with mismatched substrates, yeast and C. elegans genetics; full six-protein reconstitution

    PMID:30462332 PMID:31371435

    Open questions at the time
    • Physiological consequence of mismatch tolerance for crossover patterning not directly measured
  14. 2020 High

    Demonstrated in vivo that DMC1 binds adjacent to the break end while RAD51 binds distally, settling that DMC1 performs the strand-exchange step in mammalian meiosis, and identified BRME1 as a regulator of recombinase loading.

    Evidence Allele-specific ChIP-seq and super-resolution microscopy in hybrid mice; BRME1 conditional KO with co-IP

    PMID:32460033 PMID:32610038

    Open questions at the time
    • BRME1 finding is Medium-confidence single-lab
    • Spatial separation mechanism on resected DNA not fully explained
  15. 2021 High

    Resolved the structural basis of DMC1's mismatch tolerance and crossover bias by cryo-EM, localizing Loop1/Loop2 differences (Gln244, Pro274/Gly275 vs RAD51) that form an open triplet gate, and demonstrating fidelity swaps by residue exchange.

    Evidence Cryo-EM of pre/postsynaptic complexes, MD simulation, smFRET, mutagenesis with strand-exchange assays

    PMID:33446654 PMID:34871438

    Open questions at the time
    • How tolerance is balanced against fidelity during homology search in vivo unresolved
  16. 2023 High

    Identified FIGNL1 as a disassembly factor for DMC1 filaments, showing that filament turnover is actively required for proper synapsis and DSB repair, completing the load/activate/remove cycle.

    Evidence In vitro filament disassembly with purified FIGNL1; conditional KO mouse with cytology

    PMID:37891173

    Open questions at the time
    • Selectivity of FIGNL1 for DMC1 vs RAD51 in vivo not separated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the full accessory network (mediators, translocases, anti-recombinase inhibition, and post-translational modifications such as SUMOylation) is temporally coordinated in vivo to bias DMC1 intermediates toward interhomolog crossovers remains unresolved.
  • No integrated in vivo timeline of mediator action
  • Functional consequence of DMC1 SUMOylation in mammals untested
  • Regulation linking filament turnover to crossover designation unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140097 catalytic activity, acting on DNA 5 GO:0003677 DNA binding 3 GO:0005198 structural molecule activity 3 GO:0140657 ATP-dependent activity 3
Localization
GO:0005634 nucleus 3 GO:0005694 chromosome 3 GO:0000228 nuclear chromosome 2
Pathway
R-HSA-1474165 Reproduction 3 R-HSA-73894 DNA Repair 3 R-HSA-1640170 Cell Cycle 1
Partners
BRCA2FIGNL1HOP2MEI5MND1RAD51RAD51AP1TID1/RDH54
Complex memberships
DMC1-Mei5-Sae3 complexDMC1-ssDNA presynaptic filament

Evidence

Reading pass · 50 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1992 DMC1 encodes a meiosis-specific RecA homolog in yeast (S. cerevisiae) required for reciprocal recombination, synaptonemal complex formation, and cell cycle progression past meiotic prophase; dmc1 mutants accumulate double-strand break recombination intermediates and arrest in late meiotic prophase. Genetic analysis, mutant phenotyping, molecular cloning Cell High 1581960
1994 Dmc1 and Rad51 colocalize to as many as 64 punctate sites (foci) in spread meiotic nuclei, likely representing recombination intermediates; Dmc1 complexes fail to form in rad51 mutants, while Rad51 complexes persist indefinitely in dmc1 mutants, indicating Rad51 is required upstream of Dmc1 complex formation; Zip1 protein promotes dissociation of Dmc1 complexes. Immunostaining of spread meiotic nuclei; genetic epistasis with rad51, dmc1, zip1 mutants Cell High 7528104
1998 Mouse Dmc1 is required for homologous chromosome synapsis during meiosis in both sexes; Dmc1-null males and females are sterile, with meiotic arrest at early zygotene and failure of homolog pairing despite axial element formation. Targeted gene disruption (knockout mouse); cytological analysis of spermatocytes Molecular cell High 9660953 9660954
1999 Mouse RAD51 and DMC1 colocalize on meiotic chromosome cores at early prophase I and interact with each other and with the chromosome core component SCP3 (COR1) as shown by two-hybrid and in vitro binding assays, suggesting formation of a multiprotein recombination complex on meiotic chromosome cores. Immunofluorescence, immunoelectron microscopy, yeast two-hybrid, in vitro binding assay The Journal of cell biology Medium 10525529
1999 Human Dmc1 (hDmc1) forms octameric rings rather than helical filaments (unlike RecA and Rad51); DNA binds in the central channel of the ring, representing the likely active form. Electron microscopy (structural analysis of purified hDmc1 protein) Proceedings of the National Academy of Sciences of the United States of America Medium 10485886
2001 Purified S. cerevisiae Dmc1 has weak DNA-dependent ATPase activity, binds ssDNA and dsDNA cooperatively, renatures linearized plasmid DNA, and catalyzes strand assimilation of ssDNA into homologous supercoiled duplex DNA in an ATP-dependent or ATP-independent (AMP-PNP-supported) reaction. Protein purification, ATPase assay, EMSA, strand assimilation/renaturation assay in vitro The Journal of biological chemistry High 11551925
2004 Crystal structure of full-length human Dmc1 octameric ring resolved; the monomeric structure closely resembles Rad51 and archaeal Rad51; an additional hydrogen bonding interaction at the polymer interface (not present in Rad51) stabilizes the octameric ring over helical filaments. Mutagenesis identified inner and outer basic patches: the inner patch binds both ssDNA and dsDNA, while the outer patch binds ssDNA, suggesting a model for DNA interaction during homologous pairing. X-ray crystallography, site-directed mutagenesis, DNA binding assays Molecular cell High 15125839
2004 Human Dmc1 mediates ATP-dependent DNA strand exchange over at least several thousand base pairs between paired DNA substrates; the reaction requires RPA and initiates through nucleation of hDmc1 onto ssDNA to form a helical nucleoprotein filament. In vitro strand exchange assay with purified proteins; electron microscopy of nucleoprotein filaments Nature High 15164066
2004 Meiosis-specific proteins Mei5 and Sae3 form a ternary complex with Dmc1 and are required for assembly of Dmc1 (but not Rad51) on meiotic chromosomes and at recombination hot spots; their recruitment requires Rad51; the Dmc1-Mei5-Sae3 complex is integrated onto Rad51 ensembles. Genetic analysis (mei5, sae3 mutants), chromatin immunoprecipitation, immunostaining of meiotic chromosomes, co-immunoprecipitation Cell High 15620352
2004 The Hop2-Mnd1 heterodimer stimulates the strand assimilation activity of Dmc1 in vitro and functions in the same genetic pathway as HOP2, MND1, and DMC1 for homologous chromosome juxtaposition in S. cerevisiae; Hop2 and Mnd1 form a stable heterodimer with higher affinity for dsDNA than ssDNA. In vitro strand assimilation assay, double-mutant epistasis analysis, protein-protein interaction assays Proceedings of the National Academy of Sciences of the United States of America High 15249670
2004 Human MSH4 physically interacts with both RAD51 and DMC1 in biochemical pulldown assays, and a subset of MSH4 foci colocalize with DMC1/RAD51 complexes on mouse meiotic chromosomes. In vitro binding assay (pulldown), immunolocalization on mouse meiotic chromosomes Molecular human reproduction Medium 15489243
2005 Mouse HOP2/TBPIP stimulates DMC1-mediated homologous pairing in vitro but does not stimulate RAD51; the stimulatory effect requires HOP2 to first bind dsDNA; the C-terminal basic region of HOP2 is required for DNA binding and for pairing stimulation. In vitro homologous pairing assay with purified proteins, deletion mutagenesis, DNA binding assay The Journal of biological chemistry High 15192114
2005 Mouse Hop2-Mnd1 heterodimer physically interacts with both Rad51 and Dmc1 recombinases and stimulates their D-loop/strand invasion activity up to 35-fold; Hop2-Mnd1 stimulates Dmc1 by stabilizing ssDNA nucleoprotein complexes and facilitating dsDNA capture by the Dmc1-ssDNA filament. D-loop assay, strand invasion assay, co-immunoprecipitation, protein-protein interaction assays with purified proteins Nature structural & molecular biology High 15834424
2005 Ca2+ stimulates the DNA strand exchange activity of human Dmc1 through conformational changes that stabilize hDmc1-ssDNA filament complexes; unlike for hRad51, Ca2+ stimulation of hDmc1 does not act primarily through inhibition of ATPase activity (hDmc1 does not self-convert into a stable ADP-bound complex). In vitro strand exchange assay, ATPase assay, electron microscopy of nucleoprotein filaments The Journal of biological chemistry High 15917244
2005 Ca2+ enables yeast Dmc1 to form regular helical filaments on ssDNA and activates its strand assimilation activity; Ca2+ increases Dmc1's affinity for ATP and reduces DNA-dependent ATPase activity, supporting the view that ATP binding (not hydrolysis) is required for functional filament structure. In vitro strand assimilation assay, ATPase assay, electron microscopy of Dmc1-ssDNA filaments The Journal of biological chemistry High 16204247
2005 The N-terminal domain (residues 1–81) of human DMC1 is required for octamer formation; deletion of this domain (DMC1-82-340) produces a heptamer and abolishes both ssDNA and dsDNA binding activities. Analytical ultracentrifugation, DNA binding assays, deletion mutagenesis The Journal of biological chemistry High 15917243
2005 The N-terminal domain of DMC1 (residues 1–81) was found to be highly flexible in the octameric ring crystal structure, in contrast to the Rad51 N-terminal domain which makes specific contacts in the helical filament; this structural difference may explain distinct oligomeric forms. X-ray crystallography (crystal structure of octameric ring) — this finding is coincident with PMID 15125839 but specifically noted for N-terminal domain The Journal of biological chemistry Medium 15917243
2005 Mei5-Sae3 complex preferentially binds ssDNA, relieves RPA-imposed inhibition of Dmc1's strand assimilation and DNA binding activities, and physically interacts with RPA; Mei5-Sae3 acts as a mediator of Dmc1 assembly onto RPA-coated ssDNA. In vitro strand assimilation assay, DNA binding assay, protein-protein interaction assay with purified proteins Genetics (Tsubouchi & Roeder 2004 PMID 15579681) / Journal of Biological Chemistry (Ferrari et al. 2009 PMID 19270307) High 15579681 19270307
2006 The S. pombe Swi5-Sfr1 complex, at substoichiometric concentrations, stimulates Dmc1-mediated strand exchange on long DNA substrates; the complex overcomes RPA-mediated inhibition of Dmc1, increases the amount of Dmc1 bound to ssDNA, and preferentially stimulates ssDNA-dependent ATPase of Rad51. In vitro strand exchange assay, ssDNA-binding assay, ATPase assay with purified proteins Nature structural & molecular biology High 16921379
2006 Tid1/Rdh54 promotes dissociation of Dmc1 from nonrecombinogenic (non-DSB) chromatin sites; an activity shared by Tid1 and Rad54 is required for normal assembly of Dmc1 at DSB sites; Tid1's DNA translocase ATPase activity mediates Dmc1 removal from nonproductive chromatin. Chromatin immunoprecipitation, genetic analysis in dmc1, tid1, rad54 mutants Genes & development High 16980587
2006 Human Rad54B stabilizes the Dmc1-ssDNA nucleoprotein complex and thereby enhances Dmc1-mediated DNA strand exchange activity in vitro. In vitro DNA strand exchange assay, ssDNA binding assay with purified proteins Nucleic acids research Medium 16945962
2007 Human BRCA2 directly binds DMC1 via a distinct 26-amino-acid region (residues 2386–2411, the PhePP motif, critical residues Phe2406, Pro2408, Pro2409) that is separate from the RAD51 interaction domain; BRCA2 thus coordinates interactions with both recombinases at meiosis through distinct binding sites. Pulldown/binding assays with truncation and point mutants of BRCA2; co-immunoprecipitation The EMBO journal High 17541404
2007 A missense mutation in the L2 DNA-binding domain of mouse Dmc1 (Dmc1Mei11) abolishes strand invasion activity; in male heterozygotes, meiosis arrests in pachynema with incomplete synapsis and no crossing-over; female heterozygotes show reduced oocyte pool but partially compensate, revealing a sex difference in DMC1 dependence. Mouse mutagenesis screen, in vitro strand invasion assay with mutant protein, cytological analysis of meiosis PLoS biology High 17425408
2008 Rad51 and Dmc1 (from both human and budding yeast) form essentially identical nucleoprotein filaments with respect to persistence length, helical pitch, filament diameter, DNA base pairs per helical turn, and handedness; differences in meiotic function are therefore likely due to distinct accessory proteins rather than intrinsic filament structural differences. Comparative electron microscopy of filaments from both human and yeast proteins; quantitative structural analysis Nucleic acids research High 18535008
2008 Crystal structure of human DMC1-M200V variant in octameric ring form shows reduced protein stability; biochemical assays demonstrate the variant is moderately defective in in vitro recombination reactions; the corresponding M194V mutation in S. pombe dmc1 significantly decreases meiotic homologous recombination frequency. X-ray crystallography, in vitro recombination assay, genetic analysis in fission yeast Nucleic acids research High 18566005
2008 Purified S. pombe Rdh54 forms a complex with Dmc1 and enhances Dmc1 recombinase activity; Rdh54 also mediates efficient removal of Dmc1 from dsDNA in an ATPase-dependent manner, preventing nonproductive Dmc1-chromatin interactions. Co-immunoprecipitation with purified proteins, in vitro recombinase activity assay, dsDNA dissociation assay, ATPase mutant analysis DNA repair High 19028606
2010 DMC1-driven D-loops are substantially more resistant to dissociation by branch-migration proteins (e.g., RAD54) than RAD51-driven D-loops; this resistance may channel DMC1 recombination intermediates toward the double-strand break repair pathway (crossovers) rather than synthesis-dependent strand annealing (non-crossovers). In vitro D-loop formation and dissociation assay with purified human DMC1, RAD51, and RAD54 proteins Nature structural & molecular biology High 21151113
2011 RAD51AP1 physically associates with DMC1 via a conserved WVPP motif (distinct from its RAD51-interaction domain) and stimulates DMC1-mediated D-loop formation by enhancing the ability of the DMC1 presynaptic filament to capture duplex DNA and assemble the synaptic complex; RAD51AP1 colocalizes with a subset of DMC1 foci in mouse spermatocytes. Co-immunoprecipitation, in vitro D-loop assay, synaptic complex assay with purified proteins, immunofluorescence on mouse spermatocytes Proceedings of the National Academy of Sciences of the United States of America High 21307306
2011 RAD51AP1 interacts with DMC1 through a conserved WVPP motif in RAD51AP1 that is critical for DMC1 interaction but dispensable for RAD51 association; this motif is similar to the FVPP (PhePP) motif in BRCA2 that mediates DMC1 interaction. Truncation and point-mutation mapping of RAD51AP1 interaction sites; co-immunoprecipitation The Journal of biological chemistry Medium 21903585
2012 Using a separation-of-function Rad51 mutant retaining filament-forming but not joint-molecule (JM) activity, Rad51's JM activity is shown to be fully dispensable for meiotic recombination, while the equivalent Dmc1 mutation causes profound recombination defect; Dmc1's JM activity alone is responsible for meiotic recombination. Biochemical evidence shows Rad51 acts with Mei5-Sae3 as a Dmc1 accessory factor. Separation-of-function mutant analysis in yeast, in vitro biochemical assay of strand exchange activity Science High 22955832
2012 Purified Dmc1 and Tid1 physically interact and Tid1 stimulates Dmc1-mediated joint molecule formation in vitro; under conditions optimal for Dmc1, Rad51 is specifically stimulated by Rad54 (not Tid1), establishing Dmc1-Tid1 and Rad51-Rad54 as functionally specific pairs; Dmc1-Tid1 promotes interhomolog while Rad51-Rad54 promotes intersister strand exchange. In vitro joint molecule/D-loop assay, physical interaction assay with purified proteins The Journal of biological chemistry High 22761450
2013 Purified S. cerevisiae Dmc1 (when ATP is included during purification to prevent aggregation) forms D-loops and responds to accessory factors Rad54 and Rdh54; EM reconstruction reveals the ScDmc1-ssDNA nucleoprotein filament has 6.5 protomers per turn with a pitch of ~106 Å. Protein purification, D-loop assay, negative-stain electron microscopy with helical reconstruction DNA repair High 23769192
2014 Budding yeast Hop2-Mnd1 (using the newly identified full-length ORF including exon 3) stimulates ScDmc1 D-loop activity up to 30-fold (much greater than previously reported 3-fold); stimulation requires physiological concentrations of Ca2+ (with Mg2+ also present); stimulation of Dmc1 by Hop2-Mnd1 is specific to Dmc1 and does not extend to Rad51 in budding yeast. In vitro D-loop assay with purified proteins, Ca2+/Mg2+ titration, order-of-addition experiments The Journal of biological chemistry High 24798326
2015 Distinct DNA-binding activities of Hop2-Mnd1 mediate either stabilization of the RAD51-ssDNA presynaptic filament or stimulation of the homologous DNA pairing reaction; ATP enhances the interaction between Hop2-Mnd1 and RAD51; both Hop2 and Mnd1 C-terminal regions are required for RAD51 (and DMC1) interaction; the HOP2 p.del201Glu mutation found in XX ovarian dysgenesis diminishes functional synergy with both RAD51 and DMC1. In vitro D-loop assay, presynaptic filament stabilization assay, co-immunoprecipitation with mutant proteins, pulldown with purified proteins Nucleic acids research High 25820426
2015 Dmc1-mediated strand exchange is sensitive to mismatch location, type, and distribution; mismatches near the 5' end of the initiating strand impede strand exchange dramatically, while 3'-end mismatches have little effect; Hop2-Mnd1 stimulates Dmc1-catalyzed strand exchange on homologous DNA and with a single mismatch. FRET-based strand exchange assay with defined mismatch-containing oligonucleotides and purified Dmc1/Hop2-Mnd1 The Journal of biological chemistry High 26709229
2016 Human BRCA2 BRC repeats interact directly with DMC1; most BRC repeats stimulate DMC1 joint molecule formation; BRC repeats 1-3 bind RAD51 more tightly, while BRC repeats 6-8 bind DMC1 more tightly; BRC repeat stimulation of DMC1 operates by enhancing DMC1-ssDNA complex formation; full-length BRCA2 stimulates DMC1-mediated DNA strand exchange between RPA-ssDNA complexes and duplex DNA, acting as a mediator of DMC1. In vitro D-loop/joint molecule assay with purified proteins, BRC repeat binding assays, full-length BRCA2 biochemical reconstitution Proceedings of the National Academy of Sciences of the United States of America High 26976601
2018 Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 anti-recombinase; Dmc1 inhibits Srs2 ATP hydrolysis, preventing Srs2 from undergoing ATP-dependent translocation on Dmc1-bound recombination intermediates, thereby protecting crossover intermediates from dissociation during meiosis. Biochemical assay (ATPase), single-molecule imaging of Srs2 translocation on Dmc1 filaments Proceedings of the National Academy of Sciences of the United States of America High 30301803
2018 Rad51 and Dmc1 spontaneously self-segregate within mixed presynaptic filaments without requiring other recombination accessory proteins; Dmc1 stabilizes adjacent Rad51 filaments through cross-talk between the two recombinases. Single-molecule imaging (total internal reflection fluorescence microscopy) of fluorescently labeled Rad51 and Dmc1 The Journal of biological chemistry High 29382724
2019 In vitro reconstitution of Dmc1 recombination using six purified S. cerevisiae proteins (Dmc1, RPA, Rad51, Rdh54/Tid1, Mei5-Sae3, Hop2-Mnd1) shows each accessory protein contributes to D-loop formation; RPA plays multiple stimulatory roles including overcoming inhibitory ssDNA secondary structure, elongating D-loops, and limiting inhibitory interactions of Hop2-Mnd1 and Rdh54/Tid1 with the Dmc1-ssDNA filament; Rad51 and Dmc1 directly interact in a manner enhanced by Mei5-Sae3. In vitro D-loop reconstitution assay with six purified proteins; direct protein-protein interaction assay Nucleic acids research High 30462332
2019 Three Dmc1 lineage-specific amino acids (not present in Rad51) are responsible for Dmc1's ability to stabilize mismatch-containing heteroduplex DNA base triplets; chimeric Rad51 mutants harboring Dmc1-specific amino acids gain mismatch tolerance, while Dmc1 mutants with Rad51-specific amino acids lose it. Chimeric protein mutagenesis, in vitro strand exchange assay with mismatched substrates, genetic analysis in yeast and C. elegans Genes & development High 31371435
2020 In vivo mapping in a hybrid mouse shows DMC1 binds near the DSB site on ssDNA, while RAD51 binds away from the break; these data support DMC1 (not RAD51) performing strand exchange in mammalian meiosis. Chromatin immunoprecipitation sequencing (ChIP-seq) on individual homologous chromosomes in hybrid mouse; super-resolution microscopy Molecular cell High 32610038
2020 C19orf57/BRME1 associates with BRCA2 and MEILB2/HSF2BP (which recruit recombinases to DSBs); BRME1 knockout in mouse spermatocytes delays removal of ssDNA-binding proteins from DSB sites and impairs loading of RAD51 and DMC1 onto resected ssDNA, demonstrating BRME1 modulates localization of recombinases to meiotic DSB sites. Co-immunoprecipitation, conditional knockout mouse, immunostaining of spermatocytes Cell reports Medium 32460033
2020 ScDmc1 nucleoprotein filaments are less stable than ScRad51 filaments due to a kinetically reduced nucleation step arising from lower ssDNA affinity; ScDmc1 nucleates preferentially at ssDNA-dsDNA junctions with 5'-to-3' polarity extension; short ScRad51 patches stimulate ScDmc1 nucleation through direct protein-protein interaction between ScDmc1 and ScRad51, but not with EcRecA. Single-molecule tethered particle motion experiments, in vitro filament assembly assay, pulldown assay Proceedings of the National Academy of Sciences of the United States of America High 32404423
2021 Cryo-EM structures of human Dmc1-DNA and Rad51-DNA complexes reveal that the major conformational differences are in their Loop2 regions; V273 and D274 in RAD51 (corresponding to P274 and G275 in DMC1) are key residues controlling mismatch tolerance during strand exchange; replacing Loop2 residues with Rad51 counterparts enhances DMC1 fidelity and vice versa. Cryo-EM structure determination, molecular dynamics simulation, single-molecule FRET, site-directed mutagenesis with in vitro strand exchange assay Nucleic acids research High 34871438
2021 Cryo-EM structures of DMC1 presynaptic and postsynaptic complexes show Loop1 Gln244 (Met243 in RAD51) stabilizes DNA backbone and Loop2 Pro274/Gly275 (Val273/Asp274 in RAD51) form an open 'triplet gate' for mismatch tolerance; replacing Loop1 or Loop2 residues of DMC1 with RAD51 counterparts enhances DMC1 fidelity, confirming the structural basis for distinctive mismatch tolerance. Cryo-EM, molecular dynamics simulation, site-directed mutagenesis with in vitro functional assay Nature communications High 33446654
2021 In Arabidopsis, RAD51 physically interacts with the SMC5/6 complex and restrains SMC5/6 from inhibiting DMC1 localization to meiotic chromosomes; loss of SMC5/6 partially suppresses rad51 knockout sterility in a DMC1-dependent manner. Arabidopsis genetics (double knockout suppressor analysis), immunostaining, co-immunoprecipitation The Plant cell Medium 34009315
2023 FIGNL1 AAA+ ATPase dismantles RAD51 and DMC1 filaments on both ssDNA and dsDNA in vitro; conditional knockout of FIGNL1 in mouse germline causes accumulation of RAD51/DMC1 on meiotic chromosomes and in pre-meiotic S-phase (independently of meiotic DSBs), defective chromosome synapsis, and impaired meiotic DSB repair. Conditional knockout mouse, immunostaining of spermatocytes, in vitro filament disassembly assay with purified FIGNL1 Nature communications High 37891173
2006 In Coprinus cinereus, Lim15/Dmc1 (CcLim15) is sumoylated during meiosis via interaction with the SUMO E2 conjugating enzyme Ubc9; Ubc9 binds the C-terminus (residues 105–347) of CcLim15 containing the ATPase domain; CcLim15 and CcUbc9 colocalize in meiotic nuclei from leptotene to early pachytene. In vitro protein-protein interaction assay, co-immunoprecipitation, immunocytochemistry, in vivo and in vitro sumoylation assay The FEBS journal Medium 16879611
2005 In Coprinus cinereus, DNA topoisomerase II (CcTopII) specifically interacts with CcLim15/Dmc1 in vitro and in vivo; CcLim15 activates the relaxation/catenation activity of CcTopII in vitro; CcTopII suppresses CcLim15-dependent strand transfer; CcTopII enhances CcLim15 DNA-dependent ATPase activity while CcLim15 inhibits CcTopII ATPase; the two proteins colocalize on meiotic chromosomes from leptotene to zygotene. In vitro binding assay, co-immunoprecipitation, relaxation/strand transfer/ATPase assays, immunolocalization Nucleic acids research Medium 16221977
2005 Mei1 is epistatic to Dmc1 in mouse meiosis; double Dmc1-/-Mei1-/- mutant phenotype is identical to Mei1-/- alone, positioning Mei1 upstream of Dmc1 in the meiotic recombination pathway (consistent with Mei1 being required for DSB formation upstream of Dmc1-dependent repair). Double knockout mouse epistasis analysis; oogenesis phenotype comparison Chromosoma Medium 15928951

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1992 DMC1: a meiosis-specific yeast homolog of E. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression. Cell 1026 1581960
1998 Meiotic prophase arrest with failure of chromosome synapsis in mice deficient for Dmc1, a germline-specific RecA homolog. Molecular cell 515 9660953
1998 The mouse RecA-like gene Dmc1 is required for homologous chromosome synapsis during meiosis. Molecular cell 479 9660954
1994 RecA homologs Dmc1 and Rad51 interact to form multiple nuclear complexes prior to meiotic chromosome synapsis. Cell 414 7528104
2012 Rad51 is an accessory factor for Dmc1-mediated joint molecule formation during meiosis. Science (New York, N.Y.) 266 22955832
1999 RAD51 and DMC1 form mixed complexes associated with mouse meiotic chromosome cores and synaptonemal complexes. The Journal of cell biology 199 10525529
2000 Tid1/Rdh54 promotes colocalization of rad51 and dmc1 during meiotic recombination. Proceedings of the National Academy of Sciences of the United States of America 168 11005857
1997 Saccharomyces cerevisiae recA homologues RAD51 and DMC1 have both distinct and overlapping roles in meiotic recombination. Genes to cells : devoted to molecular & cellular mechanisms 166 9427283
1997 DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is largely independent of the RAD51 pathway. Genetics 157 9335591
2004 Human meiotic recombinase Dmc1 promotes ATP-dependent homologous DNA strand exchange. Nature 153 15164066
2005 The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic recombination. Nature structural & molecular biology 144 15834424
2001 The Rad51 and Dmc1 recombinases: a non-identical twin relationship. Trends in biochemical sciences 143 11166572
1996 The mouse and human homologs of DMC1, the yeast meiosis-specific homologous recombination gene, have a common unique form of exon-skipped transcript in meiosis. Nucleic acids research 143 8602360
2013 Meiotic crossover control by concerted action of Rad51-Dmc1 in homolog template bias and robust homeostatic regulation. PLoS genetics 128 24367271
2001 Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA. The Journal of biological chemistry 114 11551925
2004 A protein complex containing Mei5 and Sae3 promotes the assembly of the meiosis-specific RecA homolog Dmc1. Cell 113 15620352
1999 Human Dmc1 protein binds DNA as an octameric ring. Proceedings of the National Academy of Sciences of the United States of America 109 10485886
2020 The Configuration of RPA, RAD51, and DMC1 Binding in Meiosis Reveals the Nature of Critical Recombination Intermediates. Molecular cell 108 32610038
2006 The Swi5-Sfr1 complex stimulates Rhp51/Rad51- and Dmc1-mediated DNA strand exchange in vitro. Nature structural & molecular biology 104 16921379
1996 recA-like genes from three archaean species with putative protein products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces cerevisiae. Nucleic acids research 104 8668545
2007 Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous pairing. Genes & development 101 17639081
2018 DMC1 mutation that causes human non-obstructive azoospermia and premature ovarian insufficiency identified by whole-exome sequencing. Journal of medical genetics 97 29331980
1999 Sister chromatid-based DNA repair is mediated by RAD54, not by DMC1 or TID1. The EMBO journal 97 10228176
2004 Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. Molecular cell 94 15125839
2004 Heterodimeric complexes of Hop2 and Mnd1 function with Dmc1 to promote meiotic homolog juxtaposition and strand assimilation. Proceedings of the National Academy of Sciences of the United States of America 94 15249670
2004 Roles of RecA homologues Rad51 and Dmc1 during meiotic recombination. Cytogenetic and genome research 94 15467365
2008 A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments. Nucleic acids research 92 18535008
2007 Interactions between human BRCA2 protein and the meiosis-specific recombinase DMC1. The EMBO journal 91 17541404
2018 High-efficiency genome editing using a dmc1 promoter-controlled CRISPR/Cas9 system in maize. Plant biotechnology journal 84 29569825
1999 High copy number suppression of the meiotic arrest caused by a dmc1 mutation: REC114 imposes an early recombination block and RAD54 promotes a DMC1-independent DSB repair pathway. Genes to cells : devoted to molecular & cellular mechanisms 81 10526232
2004 The budding yeast mei5 and sae3 proteins act together with dmc1 during meiotic recombination. Genetics 77 15579681
2015 Small Rad51 and Dmc1 Complexes Often Co-occupy Both Ends of a Meiotic DNA Double Strand Break. PLoS genetics 76 26719980
2005 Activation of human meiosis-specific recombinase Dmc1 by Ca2+. The Journal of biological chemistry 72 15917244
2003 Crossover interference in Saccharomyces cerevisiae requires a TID1/RDH54- and DMC1-dependent pathway. Genetics 69 12702674
2006 Tid1/Rdh54 promotes dissociation of Dmc1 from nonrecombinogenic sites on meiotic chromatin. Genes & development 62 16980587
2007 A dominant, recombination-defective allele of Dmc1 causing male-specific sterility. PLoS biology 61 17425408
2005 Mei1 is epistatic to Dmc1 during mouse meiosis. Chromosoma 58 15928951
2016 BRCA2 regulates DMC1-mediated recombination through the BRC repeats. Proceedings of the National Academy of Sciences of the United States of America 57 26976601
2005 Knockdown of LIM15/DMC1 in the mushroom Coprinus cinereus by double-stranded RNA-mediated gene silencing. Microbiology (Reading, England) 56 16272388
2012 Saccharomyces cerevisiae Dmc1 and Rad51 proteins preferentially function with Tid1 and Rad54 proteins, respectively, to promote DNA strand invasion during genetic recombination. The Journal of biological chemistry 54 22761450
2011 Together yes, but not coupled: new insights into the roles of RAD51 and DMC1 in plant meiotic recombination. The Plant journal : for cell and molecular biology 54 22066484
2020 Meiosis-Specific C19orf57/4930432K21Rik/BRME1 Modulates Localization of RAD51 and DMC1 to DSBs in Mouse Meiotic Recombination. Cell reports 49 32460033
2014 Down-regulation of Rad51 activity during meiosis in yeast prevents competition with Dmc1 for repair of double-strand breaks. PLoS genetics 49 24465215
2011 The recombinases Rad51 and Dmc1 play distinct roles in DNA break repair and recombination partner choice in the meiosis of Tetrahymena. PLoS genetics 49 21483758
2005 Calcium ion promotes yeast Dmc1 activity via formation of long and fine helical filaments with single-stranded DNA. The Journal of biological chemistry 49 16204247
2009 The Mei5-Sae3 protein complex mediates Dmc1 activity in Saccharomyces cerevisiae. The Journal of biological chemistry 47 19270307
2015 Significance of ligand interactions involving Hop2-Mnd1 and the RAD51 and DMC1 recombinases in homologous DNA repair and XX ovarian dysgenesis. Nucleic acids research 45 25820426
2010 The resistance of DMC1 D-loops to dissociation may account for the DMC1 requirement in meiosis. Nature structural & molecular biology 44 21151113
2000 Dmc1 of Schizosaccharomyces pombe plays a role in meiotic recombination. Nucleic acids research 44 10908327
2004 Association between MSH4 (MutS homologue 4) and the DNA strand-exchange RAD51 and DMC1 proteins during mammalian meiosis. Molecular human reproduction 43 15489243
2019 Defining the influence of Rad51 and Dmc1 lineage-specific amino acids on genetic recombination. Genes & development 40 31371435
2007 Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51 recombinases. Nucleic acids research 39 17426123
2006 Mnd1/Hop2 facilitates Dmc1-dependent interhomolog crossover formation in meiosis of budding yeast. Molecular and cellular biology 39 16581767
2021 Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination. Nucleic acids research 37 34871438
2011 Molecular basis for enhancement of the meiotic DMC1 recombinase by RAD51 associated protein 1 (RAD51AP1). Proceedings of the National Academy of Sciences of the United States of America 37 21307306
2005 Fission yeast rad51 and dmc1, two efficient DNA recombinases forming helical nucleoprotein filaments. Molecular and cellular biology 37 15899844
2004 Positive role of the mammalian TBPIP/HOP2 protein in DMC1-mediated homologous pairing. The Journal of biological chemistry 36 15192114
2001 Identification of DMC1, a novel gene in the TOC region on 17q25.1 that shows loss of expression in multiple human cancers. Journal of human genetics 36 11281419
2021 RAD51 supports DMC1 by inhibiting the SMC5/6 complex during meiosis. The Plant cell 34 34009315
2023 Positive and negative regulators of RAD51/DMC1 in homologous recombination and DNA replication. DNA repair 33 38142595
2019 RPA resolves conflicting activities of accessory proteins during reconstitution of Dmc1-mediated meiotic recombination. Nucleic acids research 33 30462332
2009 From meiosis to postmeiotic events: uncovering the molecular roles of the meiosis-specific recombinase Dmc1. The FEBS journal 33 20015079
2021 Identification of fidelity-governing factors in human recombinases DMC1 and RAD51 from cryo-EM structures. Nature communications 32 33446654
2014 The third exon of the budding yeast meiotic recombination gene HOP2 is required for calcium-dependent and recombinase Dmc1-specific stimulation of homologous strand assimilation. The Journal of biological chemistry 32 24798326
2012 Aberrant sporogonic development of Dmc1 (a meiotic recombinase) deficient Plasmodium berghei parasites. PloS one 31 23285059
2020 Rad51 facilitates filament assembly of meiosis-specific Dmc1 recombinase. Proceedings of the National Academy of Sciences of the United States of America 29 32404423
2008 Functional interactions of meiotic recombination factors Rdh54 and Dmc1. DNA repair 29 19028606
1996 DLH1 is a functional Candida albicans homologue of the meiosis-specific gene DMC1. Genetics 29 8725225
2018 Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 antirecombinase. Proceedings of the National Academy of Sciences of the United States of America 28 30301803
2008 Structural and functional analyses of the DMC1-M200V polymorphism found in the human population. Nucleic acids research 28 18566005
2002 Molecular evolution and phylogenetic application of DMC1. Molecular phylogenetics and evolution 28 11796028
1999 Specific interaction between DNA polymerase II (PolD) and RadB, a Rad51/Dmc1 homolog, in Pyrococcus furiosus. Nucleic acids research 28 10572168
1999 Isolation of a LIM15/DMC1 homolog from the basidiomycete Coprinus cinereus and its expression in relation to meiotic chromosome pairing. Molecular & general genetics : MGG 27 10628861
2020 Super-resolution imaging of RAD51 and DMC1 in DNA repair foci reveals dynamic distribution patterns in meiotic prophase. PLoS genetics 26 32502153
2016 Disruption of dmc1 Produces Abnormal Sperm in Medaka (Oryzias latipes). Scientific reports 26 27480068
2013 Functional attributes of the Saccharomyces cerevisiae meiotic recombinase Dmc1. DNA repair 25 23769192
2007 Rad51-independent interchromosomal double-strand break repair by gene conversion requires Rad52 but not Rad55, Rad57, or Dmc1. Molecular and cellular biology 25 18039855
1996 Localization of mouse Rad51 and Lim15 proteins on meiotic chromosomes at late stages of prophase 1. Genes to cells : devoted to molecular & cellular mechanisms 25 9135082
2019 Dmc1 is a candidate for temperature tolerance during wheat meiosis. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik 24 31853574
2023 FIGNL1 AAA+ ATPase remodels RAD51 and DMC1 filaments in pre-meiotic DNA replication and meiotic recombination. Nature communications 23 37891173
2018 Food Yellow4 reprotoxicity in relation to localization of DMC1 and apoptosis in rat testes: Roles of royal jelly and cod liver oil. Ecotoxicology and environmental safety 23 30500739
2011 RAD51-associated protein 1 (RAD51AP1) interacts with the meiotic recombinase DMC1 through a conserved motif. The Journal of biological chemistry 23 21903585
2001 Strand exchange reaction in vitro and DNA-dependent ATPase activity of recombinant LIM15/DMC1 and RAD51 proteins from Coprinus cinereus. Biochemical and biophysical research communications 23 11437377
2021 Crossover-active regions of the wheat genome are distinguished by DMC1, the chromosome axis, H3K27me3, and signatures of adaptation. Genome research 22 34426514
2021 A pathogenic DMC1 frameshift mutation causes nonobstructive azoospermia but not primary ovarian insufficiency in humans. Molecular human reproduction 22 34515795
2014 Rad51/Dmc1 paralogs and mediators oppose DNA helicases to limit hybrid DNA formation and promote crossovers during meiotic recombination. Nucleic acids research 21 25414342
2003 Genetic and cytological characterization of the RecA-homologous proteins Rad51 and Dmc1 of Schizosaccharomyces pombe. Current genetics 21 12955454
2018 Spontaneous self-segregation of Rad51 and Dmc1 DNA recombinases within mixed recombinase filaments. The Journal of biological chemistry 20 29382724
2018 A putative human infertility allele of the meiotic recombinase DMC1 does not affect fertility in mice. Human molecular genetics 20 30085085
2015 Tolerance of DNA Mismatches in Dmc1 Recombinase-mediated DNA Strand Exchange. The Journal of biological chemistry 20 26709229
2005 Role of the N-terminal domain of the human DMC1 protein in octamer formation and DNA binding. The Journal of biological chemistry 20 15917243
2000 Conversion from mitosis to meiosis: morphology and expression of proliferating cell nuclear antigen (PCNA) and Dmc1 during newt spermatogenesis. Development, growth & differentiation 20 11142682
2010 Helical filaments of human Dmc1 protein on single-stranded DNA: a cautionary tale. Journal of molecular biology 19 20600108
2006 Sumoylation of a meiosis-specific RecA homolog, Lim15/Dmc1, via interaction with the small ubiquitin-related modifier (SUMO)-conjugating enzyme Ubc9. The FEBS journal 19 16879611
2006 Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein. Nucleic acids research 19 16945962
2005 Molecular visualization of the yeast Dmc1 protein ring and Dmc1-ssDNA nucleoprotein complex. Biochemistry 19 15835894
2005 DNA topoisomerase II interacts with Lim15/Dmc1 in meiosis. Nucleic acids research 19 16221977
1989 DMC1: a monoclonal antibody produced from histiocytosis X cells which reacts with the native CD1a molecule of human epidermal Langerhans cells. Hybridoma 19 2469637
2008 The cloning of Dmc1 cDNAs and a comparative study of its expression in different ploidy cyprinid fishes. Science in China. Series C, Life sciences 17 18176789
2005 Cloning of cDNAs and the differential expression of A-type cyclins and Dmc1 during spermatogenesis in the Japanese eel, a teleost fish. Developmental dynamics : an official publication of the American Association of Anatomists 16 15736222

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