Complex formation and functional versatility of Mre11 of budding yeast in recombination

Cell. 1998 Nov 25;95(5):705-16. doi: 10.1016/s0092-8674(00)81640-2.

Abstract

Meiotic recombination of S. cerevisiae contains two temporally coupled processes, formation and processing of double-strand breaks (DSBs). Mre11 forms a complex with Rad50 and Xrs2, acting as the binding core, and participates in DSB processing. Although these proteins are also involved in DSB formation, Mre11 is not necessarily holding them. The C-terminal region of Mre11 is required only for DSB formation and binds to some meiotic proteins. The N-terminal half specifies nuclease activities that are collectively required for DSB processing. Mre11 has a DNA-binding site for DSB formation and another site for DSB processing. It has two regions to bind to Rad50. Mre11 repairs methyl methanesulfonate-induced DSBs by reactions that require the nuclease activities and those that do not.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromosomes, Fungal
  • DNA Repair*
  • DNA-Binding Proteins*
  • Endodeoxyribonucleases*
  • Exodeoxyribonucleases*
  • Fungal Proteins / metabolism
  • Fungal Proteins / physiology*
  • Guinea Pigs
  • Meiosis / genetics
  • Rabbits
  • Recombination, Genetic*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • RAD50 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • XRS2 protein, S cerevisiae
  • Endodeoxyribonucleases
  • Exodeoxyribonucleases
  • MRE11 protein, S cerevisiae