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Cell. 2008 Oct 17;135(2):250-60. doi: 10.1016/j.cell.2008.09.054.

The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break.

Author information

1
The Howard Hughes Medical Institute, Department of Molecular Genetics and Microbiology, University of Texas at Austin, Austin, TX 78712, USA.

Abstract

The Mre11/Rad50 complex has been implicated in the early steps of DNA double-strand break (DSB) repair through homologous recombination in several organisms. However, the enzymatic properties of this complex are incompatible with the generation of 3' single-stranded DNA for recombinase loading and strand exchange. In thermophilic archaea, the Mre11 and Rad50 genes cluster in an operon with genes encoding a helicase, HerA, and a 5' to 3' exonuclease, NurA, suggesting a common function. Here we show that purified Mre11 and Rad50 from Pyrococcus furiosus act cooperatively with HerA and NurA to resect the 5' strand at a DNA end under physiological conditions in vitro. The 3' single-stranded DNA generated by these enzymes can be utilized by the archaeal RecA homolog RadA to catalyze strand exchange. This work elucidates how the conserved Mre11/Rad50 complex promotes DNA end resection in archaea and may serve as a model for DSB processing in eukaryotes.

PMID:
18957200
PMCID:
PMC2581932
DOI:
10.1016/j.cell.2008.09.054
[Indexed for MEDLINE]
Free PMC Article

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