The protein complex including Mre11, Rad50, and Nbs1 (MRN) functions in DNA double-strand break repair to recognize and process DNA ends as well as signal for cell cycle arrest. Amino acid sequence similarity and overall architecture make Rad50 a member of the structural maintenance of chromosome (SMC) protein family. Like SMC proteins, Rad50 function depends on ATP binding and hydrolysis. All current evidence indicates that ATP binding and hydrolysis cause architectural rearrangements in SMC protein complexes that are important for their functions in organizing DNA. In the case of the MRN complex, the functional significance of ATP binding and hydrolysis are not yet defined. Here we review the data on the ATP-dependent activities of MRN and their possible mechanistic significance. We present some speculation on the role of ATP for function of the MRN complex based on the similarities and differences in the molecular architecture of the Rad50-containing complexes and the SMC complexes condensin and cohesin.

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Keywords Cohesin, Condensin, DNA binding, DNA repair, Double-strand break repair, MRN complex, Mre11 protein, Rad50 protein, SMC protein, Saccharomyces cerevisiae, adenosine triphosphate, chromosome, cohesin, condensin, double stranded DNA, double stranded DNA break, human, modulation, nibrin, nonhuman, priority journal, protein family, protein function, protein structure, review
Persistent URL dx.doi.org/10.1007/s10577-008-9018-6, hdl.handle.net/1765/16607
Citation
Kinoshita, E, van der Linden, E, Sanchez, H, & Wyman, C. (2009). RAD50, an SMC family member with multiple roles in DNA break repair: How does ATP affect function?. Chromosome Research: the international journal for all aspects of chromosome and nuclear biology, 17(2), 277–288. doi:10.1007/s10577-008-9018-6