The human Rad50 protein, classified as a structural maintenance of chromosomes (SMC) family member, is complexed with Mre11 (R/M) and has important functions in at least two distinct double-strand break repair pathways. To find out what the common function of R/M in these pathways might be, we investigated its architecture. Scanning force microscopy showed that the complex architecture is distinct from the described SMC family members. R/M consisted of two highly flexible intramolecular coiled coils emanating from a central globular DNA binding domain. DNA end-bound R/M oligomers could tether linear DNA molecules. These observations suggest that a unified role for R/M in multiple aspects of DNA repair and chromosome metabolism is to provide a flexible, possibly dynamic, link between DNA ends.

doi.org/10.1016/S1097-2765(01)00381-1, hdl.handle.net/1765/58246
Molecular Cell
Department of Molecular Genetics

de Jager, M., Noort, J., van Gent, D., Dekker, C., Kanaar, R., & Wyman, C. (2001). Human Rad50/Mre11 is a flexible complex that can tether DNA ends. Molecular Cell, 8(5), 1129–1135. doi:10.1016/S1097-2765(01)00381-1