ArticleJournal of molecular biology2011
Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 64 citations in OpenAlex.
- Regulation of the histone H3K36 methyltransferase Set2 by the histone chaperone Spt6.Nucleic acids research · 2026Article
- Evolutionary analysis of transcription elongation factors reveals conserved and lineage-specific regulatory domains.PLoS biology · 2026Article
- Regulation of the histone H3K36 methyltransferase Set2 by the histone chaperone Spt6.bioRxiv : the preprint server for biology · 2026Article
- Evolutionary conservation and innovations of RNA polymerase II transcription elongation factors.bioRxiv : the preprint server for biology · 2026Article
- The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain.Molecular cell · 2025Article
- Genome-wide regulation of Pol II, FACT, and Spt6 occupancies by RSC in Saccharomyces cerevisiae.Gene · 2024Article
- Insights into Spt6: a histone chaperone that functions in transcription, DNA replication, and genome stability.Trends in genetics : TIG · 2023Review
- Structure and Dynamics of Compact Dinucleosomes: Analysis by Electron Microscopy and spFRET.International journal of molecular sciences · 2023Article
- Spt6 directly interacts with Cdc73 and is required for Paf1 complex occupancy at active genes in Saccharomyces cerevisiae.Nucleic acids research · 2023Article
- The conserved histone chaperone Spt6 is strongly required for DNA replication and genome stability.Cell reports · 2023Article
- Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly.Nucleic acids research · 2022Article
- The interaction between the Spt6-tSH2 domain and Rpb1 affects multiple functions of RNA Polymerase II.Nucleic acids research · 2022Article
- Article
- Targeted protein degradation reveals a direct role of SPT6 in RNAPII elongation and termination.Molecular cell · 2021Article
- What's all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domainRSC chemical biology · 2021Review
- Yeast Spt6 Reads Multiple Phosphorylation Patterns of RNA Polymerase II C-Terminal Domain In Vitro.Journal of molecular biology · 2020Article
- Spt6 is a maintenance factor for centromeric CENP-A.Nature communications · 2020Article
- RNA polymerase II-independent recruitment of SPT6L at transcription start sites in Arabidopsis.Nucleic acids research · 2019Article
- A conserved genetic interaction between Spt6 and Set2 regulates H3K36 methylation.Nucleic acids research · 2019Article
- Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction.Cell reports · 2018Article
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7 authors at 3 institutions in 1 country.
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Abstract
The conserved and essential eukaryotic protein Spt6 functions in transcription elongation, chromatin maintenance, and RNA processing. Spt6 has three characterized functions. It is a histone chaperone capable of reassembling nucleosomes, a central component of transcription elongation complexes, and is required for recruitment of RNA processing factors to elongating RNA polymerase II (RNAPII). Here, we report multiple crystal structures of the 168-kDa Spt6 protein from Saccharomyces cerevisiae that together represent essentially all of the ordered sequence. Our two structures of the ∼900-residue core region reveal a series of putative nucleic acid and protein-protein interaction domains that fold into an elongated form that resembles the bacterial protein Tex. The similarity to a bacterial transcription factor suggests that the core domain performs nucleosome-independent activities, and as with Tex, we find that Spt6 binds DNA. Unlike Tex, however, the Spt6 S1 domain does not contribute to this activity. Crystal structures of the Spt6 C-terminal region reveal a tandem SH2 domain structure composed of two closely associated SH2 folds. One of these SH2 folds is cryptic, while the other shares striking structural similarity with metazoan SH2 domains and possesses structural features associated with the ability to bind phosphorylated substrates including phosphotyrosine. Binding studies with phosphopeptides that mimic the RNAPII C-terminal domain revealed affinities typical of other RNAPII C-terminal domain-binding proteins but did not indicate a specific interaction. Overall, these findings provide a structural foundation for understanding how Spt6 encodes several distinct functions within a single polypeptide chain.
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