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Gene Review

DMC1  -  DNA meiotic recombinase 1

Homo sapiens

Synonyms: DMC1H, LIM15, Meiotic recombination protein DMC1/LIM15 homolog, dJ199H16.1
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Disease relevance of DMC1


High impact information on DMC1


Biological context of DMC1

  • Therefore, these results suggest that TBPIP/HOP2 directly binds to DNA and functions as an activator for DMC1 during the homologous pairing step in meiosis [8].
  • During mouse meiosis, the early prophase RAD51/DMC1 recombination protein sites, which are associated with the chromosome cores and which serve as markers for ongoing DNA-DNA interactions, are in ten-fold excess of the eventual reciprocal recombinant events [9].
  • The C-terminal domain (amino acid 234-340) of MmDMC1 binds to DNA-binding domain of p53 protein. p53 might be involved in homologous recombination and/or checkpoint function by directly binding to DMC1 protein to repress genomic instability in meiotic germ cells [10].
  • The overall amino acid sequence reveals characteristic elements of a RECA-like gene yet harbors an src-like phosphorylation site curiously absent from hRAD51 and hLIM15 [11].
  • The predicted amino acid sequence of the oyster mushroom gene is 62% identical to the yeast DMC1 and 60% identical to human DMC1 [12].

Anatomical context of DMC1


Associations of DMC1 with chemical compounds

  • Expression of various germ cell markers, such as Vasa, growth differentiation marker 9 and SSEA-1, increased in the clonal cell line, and OLCs showed additionally expression of meiosis-specific markers SCP3 and DMC1 [15].

Physical interactions of DMC1


Regulatory relationships of DMC1


Other interactions of DMC1

  • Intron conservation, intron gain or loss and putative intron sliding events were determined for a set of three genes (SPO11, MRE11 and DMC1) involved in basic aspects of recombination in eukaryotes [18].
  • Emerging evidence suggests that the tumor suppressor BRCA2 functions in the assembly of nucleoprotein filaments of Rad51 and Dmc1 [19].
  • We propose that the interaction between Lim15/Dmc1 and PCNA mediates the recombination-associated DNA synthesis during meiosis [20].
  • A significant inhibition of the mixed skin cell-lymphocyte reaction was obtained with BL6 and DMC1 monoclonal antibodies (MoAb), which recognize the same epitope on CD1a molecule [13].
  • Here, we show that Ubc9 interacts with the meiosis-specific RecA homolog, Lim15/Dmc1 in the basidiomycete Coprinus cinereus (CcLim15), and mediates sumoylation of CcLim15 during meiosis [21].

Analytical, diagnostic and therapeutic context of DMC1

  • Analytical ultracentrifugation experiments revealed that, whereas full-length DMC1 forms a octamer, DMC1-(82-340) is a heptamer [22].
  • Electron microscopy reveals that the human meiosis-specific recombinase Dmc1 forms ring structures that bind single-stranded (ss) and double-stranded (ds) DNA [23].
  • Sequence analysis and biochemical studies have shown that archaeal RadA proteins are more closely related to Rad51 and Dmc1 than the bacterial RecA proteins [24].
  • Analysis of protein-protein interactions using surface plasmon resonance indicates that Coprinus cinereus PCNA (CoPCNA) specifically interacts with a meiotic specific RecA-like factor, C. cinereus Lim15/Dmc1 (CoLim15) in vitro [20].
  • The amino acid sequences encoded by the PCR fragments, three RadA protein sequences previously published (21), and two new complete RadA sequences were aligned with representative bacterial RecA proteins and eucaryal Rad51 and Dmc1 proteins [25].


  1. 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. Habu, T., Taki, T., West, A., Nishimune, Y., Morita, T. Nucleic Acids Res. (1996) [Pubmed]
  2. Identification of DMC1, a novel gene in the TOC region on 17q25.1 that shows loss of expression in multiple human cancers. Harada, H., Nagai, H., Tsuneizumi, M., Mikami, I., Sugano, S., Emi, M. J. Hum. Genet. (2001) [Pubmed]
  3. DMC1: a monoclonal antibody produced from histiocytosis X cells which reacts with the native CD1a molecule of human epidermal Langerhans cells. Dezutter-Dambuyant, C., Schmitt, D., Staquet, M.J., Gaucherand, M., Cambazard, F., Thivolet, J. Hybridoma (1989) [Pubmed]
  4. Localization of RecA-like recombination proteins on chromosomes of the lily at various meiotic stages. Terasawa, M., Shinohara, A., Hotta, Y., Ogawa, H., Ogawa, T. Genes Dev. (1995) [Pubmed]
  5. RecA-like proteins are components of early meiotic nodules in lily. Anderson, L.K., Offenberg, H.H., Verkuijlen, W.M., Heyting, C. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  6. Fission yeast rad51 and dmc1, two efficient DNA recombinases forming helical nucleoprotein filaments. Sauvageau, S., Stasiak, A.Z., Banville, I., Ploquin, M., Stasiak, A., Masson, J.Y. Mol. Cell. Biol. (2005) [Pubmed]
  7. Characterization of a 500 kb region on 17q25 and the exclusion of candidate genes as the familial Tylosis Oesophageal Cancer (TOC) locus. Risk, J.M., Evans, K.E., Jones, J., Langan, J.E., Rowbottom, L., McRonald, F.E., Mills, H.S., Ellis, A., Shaw, J.M., Leigh, I.M., Kelsell, D.P., Field, J.K. Oncogene (2002) [Pubmed]
  8. Positive role of the mammalian TBPIP/HOP2 protein in DMC1-mediated homologous pairing. Enomoto, R., Kinebuchi, T., Sato, M., Yagi, H., Shibata, T., Kurumizaka, H., Yokoyama, S. J. Biol. Chem. (2004) [Pubmed]
  9. The time course and chromosomal localization of recombination-related proteins at meiosis in the mouse are compatible with models that can resolve the early DNA-DNA interactions without reciprocal recombination. Moens, P.B., Kolas, N.K., Tarsounas, M., Marcon, E., Cohen, P.E., Spyropoulos, B. J. Cell. Sci. (2002) [Pubmed]
  10. p53 Protein interacts specifically with the meiosis-specific mammalian RecA-like protein DMC1 in meiosis. Habu, T., Wakabayashi, N., Yoshida, K., Yomogida, K., Nishimune, Y., Morita, T. Carcinogenesis (2004) [Pubmed]
  11. Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis. Rice, M.C., Smith, S.T., Bullrich, F., Havre, P., Kmiec, E.B. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  12. Isolation, characterization, and expression patterns of a DMC1 homolog from the basidiomycete Pleurotus ostreatus. Mikosch, T.S., Sonnenberg, A.S., Van Griensven, L.J. Fungal Genet. Biol. (2001) [Pubmed]
  13. A potential role for CD1a molecules on human epidermal Langerhans cells in allogeneic T-cell activation. Moulon, C., Péguet-Navarro, J., Schmitt, D. J. Invest. Dermatol. (1991) [Pubmed]
  14. Molecular cloning and gene expression of Spo11 during spermatogenesis in the Japanese eel, Anguilla japonica. Ozaki, Y., Miura, C., Miura, T. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2006) [Pubmed]
  15. Derivation of oocyte-like cells from a clonal pancreatic stem cell line. Danner, S., Kajahn, J., Geismann, C., Klink, E., Kruse, C. Mol. Hum. Reprod. (2007) [Pubmed]
  16. DNA topoisomerase II interacts with Lim15/Dmc1 in meiosis. Iwabata, K., Koshiyama, A., Yamaguchi, T., Sugawara, H., Hamada, F.N., Namekawa, S.H., Ishii, S., Ishizaki, T., Chiku, H., Nara, T., Sakaguchi, K. Nucleic Acids Res. (2005) [Pubmed]
  17. DNA strand exchange activity of rice recombinase OsDmc1 monitored by fluorescence resonance energy transfer and the role of ATP hydrolysis. Rajanikant, C., Kumbhakar, M., Pal, H., Rao, B.J., Sainis, J.K. FEBS J. (2006) [Pubmed]
  18. Intron gain and loss in the evolution of the conserved eukaryotic recombination machinery. Hartung, F., Blattner, F.R., Puchta, H. Nucleic Acids Res. (2002) [Pubmed]
  19. Meiotic recombination: an affair of two recombinases. Sehorn, M.G., Sung, P. Cell Cycle (2004) [Pubmed]
  20. Proliferating cell nuclear antigen (PCNA) interacts with a meiosis-specific RecA homologues, Lim15/Dmc1, but does not stimulate its strand transfer activity. Hamada, F.N., Koshiyama, A., Namekawa, S.H., Ishii, S., Iwabata, K., Sugawara, H., Nara, T.Y., Sakaguchi, K., Sawado, T. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  21. Sumoylation of a meiosis-specific RecA homolog, Lim15/Dmc1, via interaction with the small ubiquitin-related modifier (SUMO)-conjugating enzyme Ubc9. Koshiyama, A., Hamada, F.N., Namekawa, S.H., Iwabata, K., Sugawara, H., Sakamoto, A., Ishizaki, T., Sakaguchi, K. FEBS J. (2006) [Pubmed]
  22. Role of the N-terminal domain of the human DMC1 protein in octamer formation and DNA binding. Kinebuchi, T., Kagawa, W., Kurumizaka, H., Yokoyama, S. J. Biol. Chem. (2005) [Pubmed]
  23. The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51. Masson, J.Y., Davies, A.A., Hajibagheri, N., Van Dyck, E., Benson, F.E., Stasiak, A.Z., Stasiak, A., West, S.C. EMBO J. (1999) [Pubmed]
  24. Archaeal RadA protein binds DNA as both helical filaments and octameric rings. Yang, S., Yu, X., Seitz, E.M., Kowalczykowski, S.C., Egelman, E.H. J. Mol. Biol. (2001) [Pubmed]
  25. Diversity of radA genes from cultured and uncultured archaea: comparative analysis of putative RadA proteins and their use as a phylogenetic marker. Sandler, S.J., Hugenholtz, P., Schleper, C., DeLong, E.F., Pace, N.R., Clark, A.J. J. Bacteriol. (1999) [Pubmed]
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