TY - JOUR
T1 - DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA
AU - Sung, Patrick
AU - Robberson, Donald L.
N1 - Funding Information:
Correspondence should be addressed to P. S. We thank Louise Pra-kash, Satya Prakash, and Scott Lauder for reading the manuscript and for many helpful suggestions. P. S. gratefully acknowledges Louise Prakash and Satya Prakash for advice and support. D. L. R. wishes to thank Janet Schildmeijer Robberson and Joel Newsome for assistance in electron micrograph measurements and print preparation. This work was supported by National Institutes of Health grant R01-ES07061 (to P. S.) and by the Sealy Center for Molecular Science.
PY - 1995/8/11
Y1 - 1995/8/11
N2 - Yeast RAD51 gene functions in genetic recombination and DNA double-strand break repair. In vitro, in the presence of ATP and replication protein A, RAD51 protein pairs single-stranded DNA (ssDNA) with homologous double-stranded DNA (dsDNA) and catalyzes strand exchange between the synapsed DNA partners. Electron microscopic analyses showthat RAD51 forms helical filaments on both ssDNA and dsDNA, in which the DNA is highly extended. However, results presented here indicate that only the RAD51-ssDNA nucleoprotein filament is functionally relevant. Strand exchange is arrested when heterology is encountered in the duplex partner, and analysis of the configuration of the terminal joint thus formed reveals that pairing and strand exchange initiate at the 5′ end of the complementary strand in the linear duplex, a reaction polarity opposite to that of the bacterial prototype RecA.
AB - Yeast RAD51 gene functions in genetic recombination and DNA double-strand break repair. In vitro, in the presence of ATP and replication protein A, RAD51 protein pairs single-stranded DNA (ssDNA) with homologous double-stranded DNA (dsDNA) and catalyzes strand exchange between the synapsed DNA partners. Electron microscopic analyses showthat RAD51 forms helical filaments on both ssDNA and dsDNA, in which the DNA is highly extended. However, results presented here indicate that only the RAD51-ssDNA nucleoprotein filament is functionally relevant. Strand exchange is arrested when heterology is encountered in the duplex partner, and analysis of the configuration of the terminal joint thus formed reveals that pairing and strand exchange initiate at the 5′ end of the complementary strand in the linear duplex, a reaction polarity opposite to that of the bacterial prototype RecA.
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U2 - 10.1016/0092-8674(95)90434-4
DO - 10.1016/0092-8674(95)90434-4
M3 - Article
C2 - 7634335
AN - SCOPUS:0029112483
SN - 0092-8674
VL - 82
SP - 453
EP - 461
JO - Cell
JF - Cell
IS - 3
ER -