Meiotic recombination: an affair of two recombinases.
In E. coli, homologous recombination is catalyzed by the RecA recombinase. Two RecA-like factors, Rad51 and Dmc1, are found in eukaryotes. Whereas Rad51 is needed for homologous recombination reactions in both mitotic and meiotic cells, the role of Dmc1 is restricted to meiosis. Recent work has shown that, like RecA and Rad51, Dmc1 mediates the homologous DNA pairing strand exchange reaction via a filamentous intermediate assembled on single-stranded DNA. Emerging evidence suggests that the tumor suppressor BRCA2 functions in the assembly of nucleoprotein filaments of Rad51 and Dmc1. The manner in which Rad51 and Dmc1 functionally cooperate in meiotic recombination remains to be determined.
Sehorn
Michael G
MG
Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520-8024, USA. Michael.sehorn@yale.edu
Sung
Patrick
P
D024682:BRCA2 Protein / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism* / Q000648:ultrastructure; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000378:metabolism* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000378:metabolism* / Q000648:ultrastructure; D008540:Meiosis; D008957:Models, Genetic; D051135:Rad51 Recombinase / Q000378:metabolism*; D011995:Recombination, Genetic
D024682:BRCA2 Protein; D018797:Cell Cycle Proteins; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D051135:Rad51 Recombinase; C074556:DMC1 protein, human