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J Biol Chem, Vol. 273, Issue 20, 12274-12280, May 15, 1998
DNA Strand Invasion Promoted by Escherichia coli RecT
Protein
Philippe
Noirot and
Richard D.
Kolodner
From the Division of Human Cancer Genetics, Dana Farber Cancer
Institute, and the Department of Biological Chemistry and Molecular
Pharmacology, Harvard Medical School, Boston, Massachusetts 02115
The RecT protein of Escherichia coli
is a DNA-pairing protein required for the RecA-independent
recombination events promoted by the RecE pathway. The RecT protein was
found to bind to both single-stranded DNA (ssDNA) and double-stranded
DNA (dsDNA) in the absence of Mg2+. In the presence of
Mg2+, RecT binding to dsDNA was inhibited drastically,
whereas binding to ssDNA was inhibited only to a small extent. RecT
promoted the transfer of a single-stranded oligonucleotide into a
supercoiled homologous duplex to form a D (displacement)-loop. D-loop
formation occurred in the absence of Mg2+ and at 1 mM Mg2+ but was inhibited by increasing
concentrations of Mg2+ and did not require a high energy
cofactor. Strand transfer was mediated by a RecT-ssDNA nucleoprotein
complex reacting with a naked duplex DNA and was prevented by the
formation of RecT-dsDNA nucleoprotein complexes. Finally, RecT mediated
the formation of joint molecules between a supercoiled DNA and a linear
dsDNA substrate with homologous 3'-single-stranded tails. Together
these results indicate that RecT is not a helix-destabilizing protein promoting a reannealing reaction but rather is a novel type of pairing
protein capable of promoting recombination by a DNA strand invasion
mechanism. These results are consistent with the observation that RecE (exonuclease VIII) and RecT can promote RecA-independent double-strand break repair in E. coli.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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