FIGNL1 binds DMC1, RAD51

Stable Identifier
R-HSA-9853878
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Human FIGNL1 binds to both RAD51 and DMC1 and these interactions are mediated by the FRBD (FIGNL1's RAD51 binding domain) region of FIGNL1. These interactions were also observed between Arabidopsis FIGNL1, RAD51, and DMC1. Human FIRRM (also known as FLIP or Apolo1 or C1orf112), a component of the evolutionarily conserved FIRRM:FIGNL1 complex, also binds to DMC1, suggesting that FIRRM could reinforce the interaction of the FIRRM:FIGNL1 complex with DMC1 (Fernandes et al. 2018).

While no interaction could be detected between Arabidopsis FIRRM and DMC1 orthologues, FIRRM was identified in a genetic screen as a meiotic anti-crossover factor in Arabidopsis, together with Arabidopsis FIGNL1. MUS81 (part of the class II pathway for resolution of meiotic Holliday junctions) is required for resolution of meiotic recombination intermediates formed in FIRRM1 knockout mutants in Arabidopsis, leading to formation of extra crossovers, as previously observed in FIGNL1 Arabidopsis knockouts. The FIRRM:FIGNL1 complex is thought to regulate the kinetics of appearance and disappearance of RAD51 and DMC1 foci in Arabidopsis, with FIGNL1 playing a more central role than FIRRM (Fernandes et al. 2018).
Literature References
PubMed ID Title Journal Year
29608566 FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination

Andrey, P, Kumar, R, Froger, N, Seguéla-Arnaud, M, Mercier, R, Choinard, S, Gevaert, K, Fernandes, JB, De Winne, N, Solier, V, Girard, C, Duhamel, M, Grelon, M, De Jaeger, G, Guerois, R

PLoS Genet 2018
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