4.8 Article

Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation

Journal

EMBO JOURNAL
Volume 30, Issue 14, Pages 2829-2842

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/emboj.2011.193

Keywords

H3K4 methylation; SAGA; Sgf29; Tudor

Funding

  1. Structural Genomics Consortium [1097737]
  2. Canadian Institutes for Health Research
  3. Canadian Foundation for Innovation
  4. Genome Canada through the Ontario Genomics Institute
  5. GlaxoSmithKline
  6. Karolinska Institute
  7. Knut and Alice Wallenberg Foundation
  8. Ontario Innovation Trust
  9. Ontario Ministry for Research and Innovation
  10. Merck Co., Inc.
  11. Novartis Research Foundation
  12. Swedish Agency for Innovation Systems
  13. Swedish Foundation for Strategic Research
  14. Wellcome Trust
  15. Chinese Ministry of Science and Technology [2009CB825502, 2006CB806501]
  16. Chinese Academy of Sciences
  17. National Natural Science Foundation of China [30970576]
  18. Damon Runyon Cancer Research Foundation [1751-03]
  19. NIH [GM46787, CA132878]
  20. US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]

Ask authors/readers for more resources

The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, and show that Sgf29 selectively binds H3K4me2/3 marks. Our crystal structures reveal that Sgf29 harbours unique tandem Tudor domains in its C-terminus. The tandem Tudor domains in Sgf29 tightly pack against each other face-to-face with each Tudor domain harbouring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively. The H3A1 and K4me3 binding pockets and the limited binding cleft length between these two binding pockets are the structural determinants in conferring the ability of Sgf29 to selectively recognize H3K4me2/3. Our in vitro and in vivo functional assays show that Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediates histone H3 acetylation, underscoring the importance of Sgf29 in gene regulation. The EMBO Journal ( 2011) 30, 2829-2842. doi: 10.1038/emboj.2011.193; Published online 17 June 2011

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