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


Authors: Hohl, M.; Kwon, Y.; Galván, S. M.; Xue, X.; Tous, C.; Aguilera, A.; Sung, P.; Petrini, J. H. J.
Article Title: The Rad50 coiled-coil domain is indispensable for Mre11 complex functions
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. © 2011 Nature America, Inc. All rights reserved.
Keywords: controlled study; gene mutation; nonhuman; dna recombination; telomere; mre11 protein; rad50 protein; allele; saccharomyces cerevisiae; double stranded dna break
Journal Title: Nature Structural and Molecular Biology
Volume: 18
Issue: 10
ISSN: 1545-9993
Publisher: Nature Publishing Group  
Date Published: 2011-09-04
Start Page: 1124
End Page: 1131
Language: English
DOI: 10.1038/nsmb.2116
PROVIDER: scopus
PMCID: PMC3190017
PUBMED: 21892167
DOI/URL:
Notes: --- - "Export Date: 9 December 2011" - "CODEN: NSMBC" - "Source: Scopus"
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors
  1. John Petrini
    94 Petrini
  2. Marcel Hohl
    13 Hohl