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

Marcel Hohl, Youngho Kwon, Sandra Muñoz Galván, Xiaoyu Xue, Cristina Tous, Andrés Aguilera, Patrick Sung, John H.J. Petrini

Research output: Contribution to journalArticlepeer-review

70 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1124-1131
Number of pages8
JournalNature Structural and Molecular Biology
Volume18
Issue number10
DOIs
StatePublished - Oct 2010
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint

Dive into the research topics of 'The Rad50 coiled-coil domain is indispensable for Mre11 complex functions'. Together they form a unique fingerprint.

Cite this