ArticleThe Journal of biological chemistry2011
Yeast transcription elongation factor Spt5 associates with RNA polymerase I and RNA polymerase II directly.
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 35 papers.
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Who cites it
35 citing papers in PubMed, 56 citations in OpenAlex.
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- Cryo-EM uncovers a sequential mechanism for RNA polymerase I pausing and stalling at abasic DNA lesions.Nature communications · 2025Article
- The conserved RNA-binding protein Seb1 promotes cotranscriptional ribosomal RNA processing by controlling RNA polymerase I progression.Nature communications · 2023Article
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
- The Paf1 Complex: A Keystone of Nuclear Regulation Operating at the Interface of Transcription and Chromatin.Journal of molecular biology · 2021Review
- Conserved strategies of RNA polymerase I hibernation and activation.Nature communications · 2021Article
- Coupling Between Production of Ribosomal RNA and Maturation: Just at the Beginning.Frontiers in molecular biosciences · 2021Review
- Prefoldin-like Bud27 influences the transcription of ribosomal components and ribosome biogenesis inRNA (New York, N.Y.) · 2020Article
- Identification of a novel base J binding protein complex involved in RNA polymerase II transcription termination in trypanosomes.PLoS genetics · 2020Article
- Coordinated Control of rRNA Processing by RNA Polymerase I.Trends in genetics : TIG · 2019Review
- Genetic analyses led to the discovery of a super-active mutant of the RNA polymerase I.PLoS genetics · 2019Article
- Article
- NETSeq reveals heterogeneous nucleotide incorporation by RNA polymerase I.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Architecture of the RNA polymerase II elongation complex: new insights into Spt4/5 and Elf1.Transcription · 2018Review
- Spt5 Plays Vital Roles in the Control of Sense and Antisense Transcription Elongation.Molecular cell · 2017Article
- Transcription factors that influence RNA polymerases I and II: To what extent is mechanism of action conserved?Biochimica et biophysica acta. Gene regulatory mechanisms · 2017Review
- The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.Protein science : a publication of the Protein Society · 2016Article
- 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
- The Transcription Factor THO Promotes Transcription Initiation and Elongation by RNA Polymerase I.The Journal of biological chemistry · 2016Article
- Structures and Functions of the Multiple KOW Domains of Transcription Elongation Factor Spt5.Molecular and cellular biology · 2015Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Spt5 is a transcription factor conserved in all three domains of life. Spt5 homologues from bacteria and archaea bind the largest subunit of their respective RNA polymerases. Here we demonstrate that Spt5 directly associates with RNA polymerase (Pol) I and RNA Pol II in yeast through its central region containing conserved NusG N-terminal homology and KOW domains. Deletion analysis of SPT5 supports our biochemical data, demonstrating the importance of the KOW domains in Spt5 function. Far Western blot analysis implicates A190 of Pol I as well as Rpb1 of Pol II in binding Spt5. Three additional subunits of Pol I may also participate in this interaction. One of these subunits, A49, has known roles in transcription elongation by Pol I. Interestingly, spt5 truncation mutations suppress the cold-sensitive phenotype of rpa49Δ strain, which lacks the A49 subunit in the Pol I complex. Finally, we observed that Spt5 directly binds to an essential Pol I transcription initiation factor, Rrn3, and to the ribosomal RNA. Based on these data, we propose a model in which Spt5 is recruited to the rDNA early in transcription and propose that it plays an important role in ribosomal RNA synthesis through direct binding to the Pol I complex.
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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.