The DMC1 gene encodes a 36.7 kDa nuclear protein involved in meiotic homologous recombination. This recombinase is functionally related to the yeast RAD51 and E. coli RecA genes. In contrast to RAD51, which functions in both mitotic and meiotic recombination, DMC1 works specifically in meiotic recombination. Despite this difference, the RAD51 and DMC1 recombinase are structurally similar but not identical in nature. This has led to the speculation that regulatory elements play a key role in the expression and function of these 2 recombinases.
Recent research show that the RAD51 associated protein 1 (RAD51AP1) binds not only to RAD51 but also to DMC1. Using mutations and point mutations the authors showed that RAD51AP1 contains a WVPP motif that allows DMC1 to bind at this specific site, but not RAD51.
Interestingly, BRCA2 has been shown to be required for meiosis specific recombination. Research has shown that BRCA2 contains a binding domain KVFVPPFK (a.a. 2404-2411) that has sequence similarities to the RAD51AP1 binding site which interacts with DMC1. RAD51 also binds to 2 other sites within BRCA2 (a.a. 996-2133 and a.a. 3265-3330), so it is possible that BRCA2 may play a key role in regulating the actions of both RAD51 and DMC1.
Another protein that may have an important role DMC1 in meiotic recombination is PSF (Polypyrimidine tract binding protein associated splicing factor). A recent paper in Nucleic Acid Research (PMID: 22156371) showed that PSF is expressed in testicular germ cells. PSF synergistically enhanced the formation of the synaptic complex of DMC1, ssDNA and dsDNA during homologous pairing. It appears to do this by enhancing the dsDNA capture by the DMC1-ssDNA comple, however it is not yet known how DMC1 interacts with the HOP2MND1 regulatory complex.
Novus Biologicals offers DMC1 reagents for your research needs including: