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Nse1 RING-like domain supports functions of the Smc5-Smc6 holocomplex in genome stability

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Overview

authors

  • Pebernard, S.
  • Perry, J. J. P.
  • Tainer, John
  • Boddy, Michael

publication date

  • October 2008

journal

  • Molecular Biology of the Cell  Journal

abstract

  • The Smc5-Smc6 holocomplex plays essential but largely enigmatic roles in chromosome segregation, and facilitates DNA repair. The Smc5-Smc6 complex contains six conserved non-SMC subunits. One of these, Nse1, contains a RING-like motif that often confers ubiquitin E3 ligase activity. We have functionally characterized the Nse1 RING-like motif, to determine its contribution to the chromosome segregation and DNA repair roles of Smc5-Smc6. Strikingly, whereas a full deletion of nse1 is lethal, the Nse1 RING-like motif is not essential for cellular viability. However, Nse1 RING mutant cells are hypersensitive to a broad spectrum of genotoxic stresses, indicating that the Nse1 RING motif promotes DNA repair functions of Smc5-Smc6. We tested the ability of both human and yeast Nse1 to mediate ubiquitin E3 ligase activity in vitro and found no detectable activity associated with full-length Nse1 or the isolated RING domains. Interestingly, however, the Nse1 RING-like domain is required for normal Nse1-Nse3-Nse4 trimer formation in vitro and for damage-induced recruitment of Nse4 and Smc5 to subnuclear foci in vivo. Thus, we propose that the Nse1 RING-like motif is a protein-protein interaction domain required for Smc5-Smc6 holocomplex integrity and recruitment to, or retention at, DNA lesions.

subject areas

  • Amino Acid Sequence
  • Carrier Proteins
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • Dimerization
  • Fungal Proteins
  • Humans
  • Molecular Conformation
  • Molecular Sequence Data
  • Nuclear Proteins
  • Protein Structure, Tertiary
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Sequence Homology, Amino Acid
  • Ubiquitin-Protein Ligases
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Identity

PubMed Central ID

  • PMC2555936

International Standard Serial Number (ISSN)

  • 1059-1524

Digital Object Identifier (DOI)

  • 10.1091/mbc.E08-02-0226

PubMed ID

  • 18667531
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Additional Document Info

start page

  • 4099

end page

  • 4109

volume

  • 19

issue

  • 10

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