ArticleThe Journal of biological chemistry2014
Regulation of RNA polymerase II termination by phosphorylation of Gdown1.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Structure of human cytoplasmic Pol II complex explains global transcription repression by GDOWN1.Nature communications · 2026Article
- Structure of cytoplasmic RNA polymerase II.Nature communications · 2026Article
- TTF2 as a potential biomarker and immunotherapy target in glioma diagnosis and prognosis.Scientific reports · 2026Article
- Polo-like kinase 1 maintains transcription and chromosomal accessibility during mitosis.Molecular biology of the cell · 2025Article
- Maintaining Transcriptional Specificity Through Mitosis.Annual review of genomics and human genetics · 2022Review
- The 3' Pol II pausing at replication-dependent histone genes is regulated by Mediator through Cajal bodies' association with histone locus bodies.Nature communications · 2022Article
- Article
- Nuclear export restricts Gdown1 to a mitotic function.Nucleic acids research · 2022Article
- Reconstitution of Pol II (G) responsive form of the human Mediator complex.Turkish journal of biology = Turk biyoloji dergisi · 2021Article
- Article
- A changing paradigm of transcriptional memory propagation through mitosis.Nature reviews. Molecular cell biology · 2019Review
- Application of the SSB biosensor to study in vitro transcription.Biochemical and biophysical research communications · 2018Article
- Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017Review
- Factor-dependent archaeal transcription termination.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- RNA polymerase II pausing as a context-dependent reader of the genome.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016Review
- Gdown1 Associates Efficiently with RNA Polymerase II after Promoter Clearance and Displaces TFIIF during Transcript Elongation.PloS one · 2016Article
- Mitotic Transcriptional Activation: Clearance of Actively Engaged Pol II via Transcriptional Elongation Control in Mitosis.Molecular cell · 2015Article
- Unraveling the mechanistic features of RNA polymerase II termination by the 5'-3' exoribonuclease Rat1.Nucleic acids research · 2015Article
- Manipulating archaeal systems to permit analyses of transcription elongation-termination decisions in vitro.Methods in molecular biology (Clifton, N.J.) · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Gdown1 is a substoichiometric subunit of RNA polymerase II (Pol II) that has been recently demonstrated to be involved in stabilizing promoter-proximal paused Pol II. It was shown to inhibit termination of Pol II by transcription termination factor 2 (TTF2) as well as block elongation stimulation by transcription factor IIF (TFIIF). Here, using in vitro transcription assays, we identified two functional domains in Gdown1. Although both are required to maintain a tight association with Pol II, the N- and C-terminal domains are responsible for blocking TTF2 and TFIIF, respectively. A highly conserved LPDKG motif found in the N-terminal domain of Gdown1 is also highly conserved in TTF2. Deletion of this motif eliminated the TTF2 inhibitory activity of Gdown1. We identified a phosphorylated form of Gdown1 with altered mobility in SDS-PAGE that appears during mitosis. A kinase in HeLa nuclear extract that caused the shift was partially purified. In vitro, Gdown1 phosphorylated by this kinase demonstrated reduced activity in blocking both TTF2 and TFIIF because of its reduced affinity for Pol II. Mass spectrometry identified Ser-270 as the site of this phosphorylation. An S270A mutation was not phosphorylated by the partially purified kinase, and an S270E mutation partially mimicked the properties of phospho-Gdown1. Gdown1 Ser-270 phosphorylation occurs predominately during mitosis, and we suggest that this would enable TTF2 to terminate all Pol II even if it is associated with Gdown1.
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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.