ArticleGenetics2011
Identification of a role for histone H2B ubiquitylation in noncoding RNA 3'-end formation through mutational analysis of Rtf1 in Saccharomyces cerevisiae.
Article in Genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
39 citing papers in PubMed, 54 citations in OpenAlex.
- Evolutionary analysis of transcription elongation factors reveals conserved and lineage-specific regulatory domains.PLoS biology · 2026Article
- Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription termination.Genes & development · 2026Article
- Sni445 recruits box C/D snoRNPs snR4 and snR45 to guide ribosomal RNA acetylation by Kre33.Nucleic acids research · 2026Article
- Evolutionary conservation and innovations of RNA polymerase II transcription elongation factors.bioRxiv : the preprint server for biology · 2026Article
- Histone H2B monoubiquitylation regulates elongation-to-termination transition in RNA polymerase II transcription.Communications biology · 2025Article
- Glc7/PP1 triggers Paf1 complex dissociation from RNA polymerase II to enable transcription termination.bioRxiv : the preprint server for biology · 2025Article
- Paf1C regulates the Neurospora circadian clock by promoting the transcription elongation of frequency.PLoS genetics · 2025Article
- Article
- Multiple direct and indirect roles of the Paf1 complex in transcription elongation, splicing, and histone modifications.Cell reports · 2024Article
- Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024Review
- Multiple direct and indirect roles of Paf1C in elongation, splicing, and histone post-translational modifications.bioRxiv : the preprint server for biology · 2024Article
- Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Rtf1 Transcriptionally Regulates Neonatal and Adult Cardiomyocyte Biology.Journal of cardiovascular development and disease · 2023Article
- Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Paf1 Complex: A Keystone of Nuclear Regulation Operating at the Interface of Transcription and Chromatin.Journal of molecular biology · 2021Review
- Article
- The nucleosome acidic patch directly interacts with subunits of the Paf1 and FACT complexes and controls chromatin architecture in vivo.Nucleic acids research · 2019Article
- The Paf1 Complex Broadly Impacts the Transcriptome ofGenetics · 2019Article
- RNA Polymerase II Transcription Attenuation at the Yeast DNA Repair Gene,G3 (Bethesda, Md.) · 2018Article
- The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.Molecular cell · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The conserved eukaryotic Paf1 complex regulates RNA synthesis by RNA polymerase II at multiple levels, including transcript elongation, transcript termination, and chromatin modifications. To better understand the contributions of the Paf1 complex to transcriptional regulation, we generated mutations that alter conserved residues within the Rtf1 subunit of the Saccharomyces cerevisiae Paf1 complex. Importantly, single amino acid substitutions within a region of Rtf1 that is conserved from yeast to humans, which we termed the histone modification domain, resulted in the loss of histone H2B ubiquitylation and impaired histone H3 methylation. Phenotypic analysis of these mutations revealed additional defects in telomeric silencing, transcription elongation, and prevention of cryptic initiation. We also demonstrated that amino acid substitutions within the Rtf1 histone modification domain disrupt 3'-end formation of snoRNA transcripts and identify a previously uncharacterized regulatory role for the histone H2B K123 ubiquitylation mark in this process. Cumulatively, our results reveal functionally important residues in Rtf1, better define the roles of Rtf1 in transcription and histone modification, and provide strong genetic support for the participation of histone modification marks in the termination of noncoding RNAs.
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Registered trials
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.