Molecular views of recombination proteins and their control

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Abstract
The efficient repair of double-stranded DNA breaks (DSBs) is essential for genome integrity and cell survival. Homologous recombination is one pathway that is used to repair DSBs, particularly in replicating cells, in which it is involved in avoiding the formation of tumours. Many of the enzymes that are involved in homologous recombination have been isolated by biochemical and genetic methods. One of these, RAD51, catalyses homologous pairing and strand exchange in many species, from yeast to humans. The specificity of RAD51 is enhanced by another key recombination protein that is known as RAD52, and much work has been done on the molecular structure of this protein. The tumour-suppressor proteins BRCA1 and BRCA2 colocalize with RAD51 in DNA-damage-induced nulear foci, and BRCA2 has been shown to interact directly with RAD51. The exact roles of BRCA1, BRCA2 and other proteins — such as BACH1 — in recombinational repair are not yet clear, but the recombination field is moving rapidly and we should not need to wait long for the answers.