ArticleNucleic acids research2018
The elongation factor Spn1 is a multi-functional chromatin binding protein.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Structure and function of IWS1 in transcription elongation.Nucleic acids research · 2026Article
- The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain.Molecular cell · 2025Article
- IWS1 positions downstream DNA to globally stimulate Pol II elongation.Nature communications · 2025Article
- Spt6-Spn1 interaction is required for RNA polymerase II association and precise nucleosome positioning along transcribed genes.The Journal of biological chemistry · 2025Article
- The histone chaperone Spn1 preserves chromatin protections at promoters and nucleosome positioning in open reading frames.G3 (Bethesda, Md.) · 2025Article
- Toward structural understanding of eukaryotic transcription elongation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025Review
- Article
- Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in Saccharomyces cerevisiae.Genetics · 2022Article
- Essential histone chaperones collaborate to regulate transcription and chromatin integrity.Genes & development · 2021Article
- Analytical Ultracentrifugation (AUC): An Overview of the Application of Fluorescence and Absorbance AUC to the Study of Biological Macromolecules.Current protocols in molecular biology · 2020Article
- The conserved elongation factor Spn1 is required for normal transcription, histone modifications, and splicing in Saccharomyces cerevisiae.Nucleic acids research · 2020Article
- Methods review: Mass spectrometry analysis of RNAPII complexes.Methods (San Diego, Calif.) · 2019Review
- Structure of transcribing RNA polymerase II-nucleosome complex.Nature communications · 2018Article
- Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction.Cell reports · 2018Article
- Article
- An undergraduate research experience in CRISPR-Cas9 mediated eukaryotic genome editing to teach fundamental biochemistry techniques.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular BiologyArticle
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The process of transcriptional elongation by RNA polymerase II (RNAPII) in a chromatin context involves a large number of crucial factors. Spn1 is a highly conserved protein encoded by an essential gene and is known to interact with RNAPII and the histone chaperone Spt6. Spn1 negatively regulates the ability of Spt6 to interact with nucleosomes, but the chromatin binding properties of Spn1 are largely unknown. Here, we demonstrate that full length Spn1 (amino acids 1-410) binds DNA, histones H3-H4, mononucleosomes and nucleosomal arrays, and has weak nucleosome assembly activity. The core domain of Spn1 (amino acids 141-305), which is necessary and sufficient in Saccharomyces cerevisiae for growth under ideal growth conditions, is unable to optimally interact with histones, nucleosomes and/or DNA and fails to assemble nucleosomes in vitro. Although competent for binding with Spt6 and RNAPII, the core domain derivative is not stably recruited to the CYC1 promoter, indicating chromatin interactions are an important aspect of normal Spn1 functions in vivo. Moreover, strong synthetic genetic interactions are observed with Spn1 mutants and deletions of histone chaperone genes. Taken together, these results indicate that Spn1 is a histone binding factor with histone chaperone functions.
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