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DNA repair and global sumoylation are regulated by distinct Ubc9 noncovalent complexes

Academic Article
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Overview

authors

  • Prudden, J.
  • Perry, J. J. P.
  • Nie, M. H.
  • Vashisht, A. A.
  • Arvai, A. S.
  • Hitomi, C.
  • Guenther, G.
  • Wohlschlegel, J. A.
  • Tainer, John
  • Boddy, Michael

publication date

  • June 2011

journal

  • Molecular and Cellular Biology  Journal

abstract

  • Global sumoylation, SUMO chain formation, and genome stabilization are all outputs generated by a limited repertoire of enzymes. Mechanisms driving selectivity for each of these processes are largely uncharacterized. Here, through crystallographic analyses we show that the SUMO E2 Ubc9 forms a noncovalent complex with a SUMO-like domain of Rad60 (SLD2). Ubc9:SLD2 and Ubc9:SUMO noncovalent complexes are structurally analogous, suggesting that differential recruitment of Ubc9 by SUMO or Rad60 provides a novel means for such selectivity. Indeed, deconvoluting Ubc9 function by disrupting either the Ubc9:SLD2 or Ubc9:SUMO noncovalent complex reveals distinct roles in facilitating sumoylation. Ubc9:SLD2 acts in the Nse2 SUMO E3 ligase-dependent pathway for DNA repair, whereas Ubc9:SUMO instead promotes global sumoylation and chain formation, via the Pli1 E3 SUMO ligase. Moreover, this Pli1-dependent SUMO chain formation causes the genome instability phenotypes of SUMO-targeted ubiquitin ligase (STUbL) mutants. Overall, we determine that, unexpectedly, Ubc9 noncovalent partner choice dictates the role of sumoylation in distinct cellular pathways.

subject areas

  • Blotting, Western
  • Carrier Proteins
  • Chromosomal Proteins, Non-Histone
  • Crystallography, X-Ray
  • DNA Repair
  • Humans
  • Mass Spectrometry
  • Models, Molecular
  • Mutation
  • Protein Structure, Quaternary
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Sumoylation
  • Ubiquitin-Conjugating Enzymes
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Identity

PubMed Central ID

  • PMC3133251

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.05188-11

PubMed ID

  • 21444718
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Additional Document Info

start page

  • 2299

end page

  • 2310

volume

  • 31

issue

  • 11

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