Human Rad50/Mre11 is a flexible complex that can tether DNA ends

Mol Cell. 2001 Nov;8(5):1129-35. doi: 10.1016/s1097-2765(01)00381-1.

M de Jager ¹, J van Noort, D C van Gent, C Dekker, R Kanaar, C Wyman

Affiliations

Affiliation

1 Department of Cell Biology and Genetics, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, Rotterdam, The Netherlands.

PMID: 11741547 DOI: 10.1016/s1097-2765(01)00381-1

Abstract

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.

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