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TitleConformational flexibility and subunit arrangement of the modular yeast Spt-Ada-Gcn5 acetyltransferase complex.
Journal, issue, pagesJ Biol Chem, Vol. 290, Issue 16, Page 10057-10070, Year 2015
Publish dateApr 17, 2015
AuthorsDheva Setiaputra / James D Ross / Shan Lu / Derrick T Cheng / Meng-Qiu Dong / Calvin K Yip /
PubMed AbstractThe Spt-Ada-Gcn5 acetyltransferase (SAGA) complex is a highly conserved, 19-subunit histone acetyltransferase complex that activates transcription through acetylation and deubiquitination of ...The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex is a highly conserved, 19-subunit histone acetyltransferase complex that activates transcription through acetylation and deubiquitination of nucleosomal histones in Saccharomyces cerevisiae. Because SAGA has been shown to display conformational variability, we applied gradient fixation to stabilize purified SAGA and systematically analyzed this flexibility using single-particle EM. Our two- and three-dimensional studies show that SAGA adopts three major conformations, and mutations of specific subunits affect the distribution among these. We also located the four functional modules of SAGA using electron microscopy-based labeling and transcriptional activator binding analyses and show that the acetyltransferase module is localized in the most mobile region of the complex. We further comprehensively mapped the subunit interconnectivity of SAGA using cross-linking mass spectrometry, revealing that the Spt and Taf subunits form the structural core of the complex. These results provide the necessary restraints for us to generate a model of the spatial arrangement of all SAGA subunits. According to this model, the chromatin-binding domains of SAGA are all clustered in one face of the complex that is highly flexible. Our results relate information of overall SAGA structure with detailed subunit level interactions, improving our understanding of its architecture and flexibility.
External linksJ Biol Chem / PubMed:25713136 / PubMed Central
MethodsEM (single particle)
Resolution38.9 - 45.3 Å
Structure data

EMDB-6299:
S. cerevisiae SAGA complex in the arched conformation
Method: EM (single particle) / Resolution: 45.3 Å

EMDB-6300:
S. cerevisiae SAGA complex in the curved conformation
Method: EM (single particle) / Resolution: 41.7 Å

EMDB-6301:
S. cerevisiae SAGA complex in the donut conformation
Method: EM (single particle) / Resolution: 38.9 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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