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The Rad50 coiled-coil domain is indispensable for Mre11 complex functions.

The Mre11 complex (Mre11, Rad50 and Xrs2 in Saccharomyces cerevisiae) influences diverse functions in the DNA damage response. The complex comprises the globular DNA-binding domain and the Rad50 hook domain, which are linked by a long and extended Rad50 coiled-coil domain. In this study, we constructed rad50 alleles encoding truncations of the coiled-coil domain to determine which Mre11 complex functions required the full length of the coils. These mutations abolished telomere maintenance and meiotic double-strand break (DSB) formation, and severely impaired homologous recombination, indicating a requirement for long-range action. Nonhomologous end joining, which is probably mediated by the globular domain of the Mre11 complex, was also severely impaired by alteration of the coiled-coil and hook domains, providing the first evidence of their influence on this process. These data show that functions of Mre11 complex are integrated by the coiled coils of Rad50.

Pubmed ID: 21892167

Authors

  • Hohl M
  • Kwon Y
  • Galván SM
  • Xue X
  • Tous C
  • Aguilera A
  • Sung P
  • Petrini JH

Journal

Nature structural & molecular biology

Publication Data

October 10, 2011

Associated Grants

  • Agency: NIEHS NIH HHS, Id: ES07061
  • Agency: NIGMS NIH HHS, Id: GM56888
  • Agency: NIGMS NIH HHS, Id: R01 GM056888
  • Agency: NIGMS NIH HHS, Id: R01 GM056888-14

Mesh Terms

  • Chromatids
  • DNA End-Joining Repair
  • DNA-Binding Proteins
  • Endodeoxyribonucleases
  • Exodeoxyribonucleases
  • Mutation
  • Recombination, Genetic
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins