SAGA-associated factor

spinqualitylabelsall models Structure of SGF11 (pink) in the SAGA complex with Sus1 (green) , SGF73 (magenta), ubiquitin (yellow), UB8P (grey), glycerol and Zn+2 ions (grey) (PDB entry 3mhs) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D SAGA-associated factor (SGF) is part of the coactivator complex SAGA (Spt-Ada-Gcn5-Acetyl transferase) which facilitates transcription of stress-activated genes. SGF29 binds methylated lysine of histone H3 and is involved in transcriptional regulation. SGF11 is required for the deubiuqitination of histone H2B and for the maintenance of steady-state H3 methylation level. SGF73 is required for the assembly of RITS complex in yeast. .

3D structures of SAGA-associated factor

Updated on 22-August-2016

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• SGF11
  • 2lo2 – ySGF zinc finger domain – yeast – NMR
    
  • 3kik, 3kjl – ySGF Sus1-binding domain + Sus1
    
  • 3mhh, 3m99, 4fip, 4fjc, 4fk5, 4wa6 – yUBP8 + Sus1 +SGF73 - yeast
    
  • 3mhs – yUBP8 + Sus1 +SGF73 + ubiquitin
    
  • 4w4u – ySGF11 + SUS1+ SGF73 (mutant) + ubiquitin carboxyl terminal hydrolase
    
  • 4zux – yUBP8 + SUS1 + SGF11 +SGF73 + ubiquitin + histone H3.2, H4, H2A, H2B + DNA
    
• SGF29
  • 3me9, 3mea, 3met, 3meu, 3mev, 3mew, 3mp1, 3mp6, 5c0m – hSGF tudor domain + histone H3 peptide – human
    
  • 3lx7, 3mp8 - hSGF tudor domain
    
• SGF73
  • 2lo3 – ySGF zinc finger domain – NMR
    

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Michal Harel, Joel L. Sussman