ArticleThe EMBO journal2011
Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.
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Who cites it
164 citing papers in PubMed, 273 citations in OpenAlex.
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- Divergent SAGA complexes shape the Toxoplasma transcriptome for lytic cycle progression and host interaction.Nature communications · 2026Article
- Epigenetic mechanisms of inflammatory memory in the central nervous system.Nature immunology · 2026Review
- Sgf29 regulates pluripotency by maintaining chromatin accessibility and promoting the expression of core transcription factors.Science China. Life sciences · 2026Article
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- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- SAGA/ATAC complexes sustain aberrant chromatin regulation and promote tumorigenesis in diffuse midline glioma.bioRxiv : the preprint server for biology · 2026Article
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- Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module.Molecular cell · 2025Article
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- Histone probes for reader and eraser investigations.Chemical science · 2025Review
- Evaluation of Cooperative Binding of Histone Post-Translational Modifications and the Surrounding Sequence by Trimethyllysine Reader Proteins.Biochemistry · 2025Article
- Discovery and mechanism of a highly selective, antifungal acetyl-CoA synthetase inhibitor.Nature communications · 2025Article
- Role of Histone H3 Lysine 4 Methylation in Chromatin Biology.Molecules (Basel, Switzerland) · 2025Review
- New breast cancer marker BF-09 is overexpressed in tumor extracts and secreted in serum.Biochemistry and biophysics reports · 2025Article
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- Potential role of lysine acetylation in the stepwise adaptation ofMicrobiology spectrum · 2025Article
104 more citing papers are in PubMed but not listed here.
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Authors and funding
19 authors at 8 institutions in 3 countries.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.