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

Chuanbing Bian, Chao Xu, Jianbin Ruan, Kenneth K. Lee, Tara L. Burke, Wolfram Tempel, Dalia Barsyte, Jing Li, Minhao Wu, Bo O. Zhou, Brian E. Fleharty, Ariel Paulson, Abdellah Allali-Hassani, Jin Qiu Zhou, Georges Mer, Patrick A. Grant, Jerry L. Workman, Jianye Zang, Jinrong Min

Research output: Contribution to journalArticlepeer-review

151 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)2829-2842
Number of pages14
JournalEMBO Journal
Issue number14
StatePublished - Jul 20 2011


  • H3K4 methylation
  • SAGA
  • Sgf29
  • Tudor

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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