Tethering on the brink: the evolutionarily conserved Mre11-Rad50 complex

Trends Biochem Sci. 2002 Aug;27(8):410-8. doi: 10.1016/s0968-0004(02)02144-8.


Mre11-Rad50 (MR) proteins are encoded by bacteriophage, eubacterial, archeabacterial and eukaryotic genomes, and form a complex with a remarkable protein architecture. This complex is capable of tethering the ends of DNA molecules, possesses a variety of DNA nuclease, helicase, ATPase and annealing activities, and performs a wide range of functions within cells. It is required for meiotic recombination, double-strand break repair, processing of mis-folded DNA structures and maintaining telomere length. This article reviews current knowledge of the structure and enzymatic activities of the MR complex and attempts to integrate biochemical information with the roles of the protein in a cell.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Conserved Sequence
  • Crystallography
  • DNA Repair
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Endodeoxyribonucleases / chemistry
  • Endodeoxyribonucleases / genetics
  • Endodeoxyribonucleases / metabolism*
  • Evolution, Molecular*
  • Exodeoxyribonucleases / chemistry
  • Exodeoxyribonucleases / genetics
  • Exodeoxyribonucleases / metabolism*
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Humans
  • MRE11 Homologue Protein
  • Molecular Sequence Data
  • Protein Conformation
  • Saccharomyces cerevisiae Proteins*
  • Telomere


  • DNA-Binding Proteins
  • Fungal Proteins
  • MRE11 protein, human
  • RAD50 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Endodeoxyribonucleases
  • Exodeoxyribonucleases
  • MRE11 Homologue Protein
  • MRE11 protein, S cerevisiae