Recombinases have a central role in
homologous recombination in a wide range of organisms. Such recombinases have been described in
archaea,
bacteria,
eukaryotes and
viruses.
Archaea The archaeon
Sulfolobus solfataricus RadA recombinase catalyzes
DNA pairing and strand exchange, central steps in recombinational repair. The RadA recombinase has greater similarity to the eukaryotic
Rad51 recombinase than to the bacterial RecA recombinase.
Eukaryotes Eukaryotic
Rad51 and its related family members are homologous to the archaeal RadA and bacterial RecA recombinases. Rad51 is highly conserved from yeast to humans. It has a key function in the recombinational repair of DNA damages, particularly double-strand damages such as double-strand breaks. In humans, over- or under-
expression of Rad51 occurs in a wide variety of
cancers. During
meiosis Rad51 interacts with another recombinase,
Dmc1, to form a presynaptic filament that is an intermediate in
homologous recombination. Dmc1 function appears to be limited to meiotic recombination. Like Rad51, Dmc1 is homologous to bacterial RecA.
Viruses Some DNA viruses encode a recombinase that facilitates homologous recombination. A well-studied example is the UvsX recombinase encoded by
bacteriophage T4. UvsX is homologous to bacterial RecA. UvsX, like RecA, can facilitate the assimilation of linear single-stranded DNA into an homologous DNA duplex to produce a
D-loop. ==References==