ArticleMolecular and cellular biology2015
Structures and Functions of the Multiple KOW Domains of Transcription Elongation Factor Spt5.
Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Spt5's central KOW domains and the Pol II stalk collaborate to regulate chromatin and 3'-end processing in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription termination.Genes & development · 2026Article
- Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription termination.bioRxiv : the preprint server for biology · 2025Article
- NusG-Spt5 Transcription Factors: Universal, Dynamic Modulators of Gene Expression.Journal of molecular biology · 2025Review
- Concerted transformation of a hyper-paused transcription complex and its reinforcing protein.Nature communications · 2024Article
- Article
- Setting Up a Better Infection: Overexpression of the Early Bacteriophage T4 GenePHAGE (New Rochelle, N.Y.) · 2022Article
- Metamorphic proteins under a computational microscope: Lessons from a fold-switching RfaH protein.Computational and structural biotechnology journal · 2022Review
- Structural basis of nucleosome transcription mediated by Chd1 and FACT.Nature structural & molecular biology · 2021Article
- Overexpression of the Bacteriophage T4Viruses · 2021Article
- Dynamics of RNA polymerase II and elongation factor Spt4/5 recruitment during activator-dependent transcription.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp.Nature structural & molecular biology · 2017Article
- RNA-dependent chromatin association of transcription elongation factors and Pol II CTD kinases.eLife · 2017Article
- A meiosis-specific Spt5 homolog involved in non-coding transcription.Nucleic acids research · 2017Article
- Spt5 Plays Vital Roles in the Control of Sense and Antisense Transcription Elongation.Molecular cell · 2017Article
- Identification of Regions in the Spt5 Subunit of DRB Sensitivity-inducing Factor (DSIF) That Are Involved in Promoter-proximal Pausing.The Journal of biological chemistry · 2017Article
- The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.Protein science : a publication of the Protein Society · 2016Article
- Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.The EMBO journal · 2016Article
- Transcription Regulation in Archaea.Journal of bacteriology · 2016Review
- Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest.The Journal of biological chemistry · 2016Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The eukaryotic Spt4-Spt5 heterodimer forms a higher-order complex with RNA polymerase II (and I) to regulate transcription elongation. Extensive genetic and functional data have revealed diverse roles of Spt4-Spt5 in coupling elongation with chromatin modification and RNA-processing pathways. A mechanistic understanding of the diverse functions of Spt4-Spt5 is hampered by challenges in resolving the distribution of functions among its structural domains, including the five KOW domains in Spt5, and a lack of their high-resolution structures. We present high-resolution crystallographic results demonstrating that distinct structures are formed by the first through third KOW domains (KOW1-Linker1 [K1L1] and KOW2-KOW3) of Saccharomyces cerevisiae Spt5. The structure reveals that K1L1 displays a positively charged patch (PCP) on its surface, which binds nucleic acids in vitro, as shown in biochemical assays, and is important for in vivo function, as shown in growth assays. Furthermore, assays in yeast have shown that the PCP has a function that partially overlaps that of Spt4. Synthesis of our results with previous evidence suggests a model in which Spt4 and the K1L1 domain of Spt5 form functionally overlapping interactions with nucleic acids upstream of the transcription bubble, and this mechanism may confer robustness on processes associated with transcription elongation.
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