ArticleThe Journal of biological chemistry2011
Solution structure of tandem SH2 domains from Spt6 protein and their binding to the phosphorylated RNA polymerase II C-terminal domain.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- A Revision of Herpes Simplex Virus Type 1 Transcription: First, Repress; Then, Express.Microorganisms · 2024Review
- Insights into Spt6: a histone chaperone that functions in transcription, DNA replication, and genome stability.Trends in genetics : TIG · 2023Review
- Spt6 directly interacts with Cdc73 and is required for Paf1 complex occupancy at active genes in Saccharomyces cerevisiae.Nucleic acids research · 2023Article
- 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
- Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs.Protein science : a publication of the Protein Society · 2018Article
- Acetylation-Dependent Recruitment of the FACT Complex and Its Role in Regulating Pol II Occupancy Genome-Wide inGenetics · 2018Article
- MicroScale Thermophoresis as a Tool to Study Protein-peptide Interactions in the Context of Large Eukaryotic Protein Complexes.Bio-protocol · 2017Article
- Article
- Paf1 Has Distinct Roles in Transcription Elongation and Differential Transcript Fate.Molecular cell · 2017Article
- Spt6 Is Essential for rRNA Synthesis by RNA Polymerase I.Molecular and cellular biology · 2015Article
- Histone deacetylases and phosphorylated polymerase II C-terminal domain recruit Spt6 for cotranscriptional histone reassembly.Molecular and cellular biology · 2014Article
- Spt6 regulates intragenic and antisense transcription, nucleosome positioning, and histone modifications genome-wide in fission yeast.Molecular and cellular biology · 2013Article
- Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3.Scientific reports · 2013Article
- Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Cell communication and signaling : CCS · 2012Article
- The histone chaperone Spt6 is required for activation-induced cytidine deaminase target determination through H3K4me3 regulation.The Journal of biological chemistry · 2012Article
- Modular evolution of phosphorylation-based signalling systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Evolution of SH2 domains and phosphotyrosine signalling networks.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Fcp1 dephosphorylation of the RNA polymerase II C-terminal domain is required for efficient transcription of heat shock genes.Molecular and cellular biology · 2012Article
- Making sense of transcribing chromatin.Current opinion in cell biology · 2012Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spt6 is a highly conserved transcription elongation factor and histone chaperone. It binds directly to the RNA polymerase II C-terminal domain (RNAPII CTD) through its C-terminal region that recognizes RNAPII CTD phosphorylation. In this study, we determined the solution structure of the C-terminal region of Saccharomyces cerevisiae Spt6, and we discovered that Spt6 has two SH2 domains in tandem. Structural and phylogenetic analysis revealed that the second SH2 domain was evolutionarily distant from canonical SH2 domains and represented a novel SH2 subfamily with a novel binding site for phosphoserine. In addition, NMR chemical shift perturbation experiments demonstrated that the tandem SH2 domains recognized Tyr(1), Ser(2), Ser(5), and Ser(7) phosphorylation of RNAPII CTD with millimolar binding affinities. The structural basis for the binding of the tandem SH2 domains to different forms of phosphorylated RNAPII CTD and its physiological relevance are discussed. Our results also suggest that Spt6 may use the tandem SH2 domain module to sense the phosphorylation level of RNAPII CTD.
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