The Rad50, Mre11 and Nbs1 complex is involved in many essential chromosomal organization processes dealing with DNA ends, including two major pathways of DNA double-strand break repair, homologous recombination and non-homologous end joining. Previous data on the structure of the human Rad50 and Mre11 (R/M) complex suggest that a common role for the protein complex in these processes is to provide a physical link between DNA ends such that they can be processed in an organized and coordinated manner. Here we describe the DNA binding properties of the R/M complex. The complex bound to both single-stranded and double-stranded DNA. Scanning force microscopy analysis of DNA binding by R/M showed the requirement for an end to form oligomeric R/M complexes, which could then migrate or transfer away from the end. The R/M complex had a lower preference for DNA substrates with 3'-overhangs compared with blunt ends or 5'-overhangs. Interestingly, ATP binding, but not hydrolysis, increased the preference of R/M binding to DNA substrates with 3'-overhangs relative to substrates with blunt ends and 5'-overhangs.

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Keywords *DNA Repair Enzymes, Adenosine Triphosphate/metabolism/*pharmacology, Animals, Cell Line, DNA, Single-Stranded/metabolism, DNA-Binding Proteins/isolation & purification/*metabolism, DNA/*metabolism/ultrastructure, Humans, Macromolecular Substances, Microscopy, Atomic Force, Protein Binding, Research Support, Non-U.S. Gov't
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de Jager, M., Wyman, C., van Gent, D.C., & Kanaar, R.. (2002). DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP. Nucleic Acids Research. Retrieved from