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Visualization of recombination intermediates produced by RAD52‐mediated single‐strand annealing
Author(s) -
Van Dyck Eric,
Stasiak Alicja Z,
Stasiak Andrzej,
West Stephen C
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve201
Subject(s) - rad52 , heteroduplex , homologous recombination , replication protein a , biology , dna , dna repair , flp frt recombination , dna replication , genetic recombination , microbiology and biotechnology , rad51 , genetics , recombination , chemistry , dna binding protein , gene , transcription factor
Double‐strand breaks (DSBs) occur frequently during DNA replication. They are also caused by ionizing radiation, chemical damage or as part of the series of programmed events that occur during meiosis. In yeast, DSB repair requires RAD52, a protein that plays a critical role in homologous recombination. Here we describe the actions of human RAD52 protein in a model system for single‐strand annealing (SSA) using tailed (i.e. exonuclease resected) duplex DNA molecules. Purified human RAD52 protein binds resected DSBs and promotes associations between complementary DNA termini. Heteroduplex intermediates of these recombination reactions have been visualized by electron microscopy, revealing the specific binding of multiple rings of RAD52 to the resected termini and the formation of large protein complexes at heteroduplex joints formed by RAD52‐mediated annealing.