The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties

Jacques Bonnet, Ying Hui Wang, Gianpiero Spedale, R. Andrew Atkinson, Christophe Romier, Ali Hamiche, W. W.M.Pim Pijnappel, H. Th Marc Timmers, Lśszló Tora, Didier Devys, Bruno Kieffer

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21 Citations (Scopus)

Abstract

SAGA (Spt-Ada-Gcn5 acetyltransferase), a coactivator complex involved in chromatin remodelling, harbours both histone acetylation and deubiquitination activities. ATXN7/Sgf73 and ATXN7L3, two subunits of the SAGA deubiquitination module, contain an SCA7 domain characterized by an atypical zinc-finger. We show that the yeast Sgf73-SCA7 domain is not required to recruit Sgf73 into SAGA. Instead, it binds to nucleosomes, a property that is conserved in the human ATXN7-SCA7 domain but is lost in the ATXN7L3 domain. The solution structures of the SCA7 domain of both ATXN7 and ATXN7L3 reveal a new, common zinc-finger motif at the heart of two distinct folds, providing a molecular basis for the observed functional differences.

Original languageEnglish
Pages (from-to)612-618
Number of pages7
JournalEMBO Reports
Volume11
Issue number8
DOIs
Publication statusPublished - Aug 2010
Externally publishedYes

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Keywords

  • ATXN7
  • nucleosome
  • SAGA
  • ubiquitin
  • zinc-finger

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Bonnet, J., Wang, Y. H., Spedale, G., Atkinson, R. A., Romier, C., Hamiche, A., Pijnappel, W. W. M. P., Timmers, H. T. M., Tora, L., Devys, D., & Kieffer, B. (2010). The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties. EMBO Reports, 11(8), 612-618. https://doi.org/10.1038/embor.2010.98