Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 19, Pages 6867-6872Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0409496102
Keywords
homologous recombination; recombination-dependent repair; RecG helicase; RuvABC resolvasome; tyrosine recombinase
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Funding
- NIAID NIH HHS [R01 AI058253] Funding Source: Medline
- NIGMS NIH HHS [R01 GM052847] Funding Source: Medline
- PHS HHS [R01-52847] Funding Source: Medline
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Holliday junctions (HJ) are the central intermediates in both homologous recombination and site-specific recombination performed by tyrosine recombinases such as the bacteriophage x Integrase (Int) protein. Previously, our lab identified peptide inhibitors of Int-mediated recombination that prevent the resolution of HJ intermediates. We now show that two of these inhibitors bind HJ DNA in the square-planar conformation even in the absence of Int protein. The peptides prevent unwinding of branched DNA substrates by the RecG helicase of Escherichia coli and interfere with the resolution of HJ substrates by the RuvABC complex. Our results suggest that these peptides target all proteins that process HJ in the square-planar conformation. These inhibitors should be extremely useful for dissecting homologous recombination and recombination-dependent repair in vitro and in vivo.
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