ArticleThe Journal of biological chemistry2014
Functional interactions of the RNA polymerase II-interacting proteins Gdown1 and TFIIF.
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 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Nuclear-targeted GDOWN1 potently suppresses tumors by inducing premature transcription termination and exporting Pol Ⅱ CTD phosphatases to activate RB.Cell death and differentiation · 2026Article
- Structure of human cytoplasmic Pol II complex explains global transcription repression by GDOWN1.Nature communications · 2026Article
- Nuclear export restricts Gdown1 to a mitotic function.Nucleic acids research · 2022Article
- Nucleotide Loading Modes of Human RNA Polymerase II as Deciphered by Molecular Simulations.Biomolecules · 2020Article
- Architecture of Pol II(G) and molecular mechanism of transcription regulation by Gdown1.Nature structural & molecular biology · 2018Article
- Born to run: control of transcription elongation by RNA polymerase II.Nature reviews. Molecular cell biology · 2018Review
- Super elongation complex contains a TFIIF-related subcomplex.Transcription · 2016Article
- Gdown1 Associates Efficiently with RNA Polymerase II after Promoter Clearance and Displaces TFIIF during Transcript Elongation.PloS one · 2016Article
- Getting up to speed with transcription elongation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Gdown1, the substoichiometric 13th subunit of RNA polymerase II (pol II), has an important role in pausing during the initial stage of transcript elongation. However, Gdown1 quantitatively displaces the essential initiation factor TFIIF from free pol II and elongating pol II. Thus, it is not clear how or even if pol II can initiate in the presence of Gdown1. Using an in vitro transcription system with purified factors and pol II lacking Gdown1, we found that although Gdown1 is strongly inhibitory to transcription when prebound to pol II, a fraction of complexes do remain active. Surprisingly, when Gdown1 is added to complete preinitiation complexes (PICs), it does not inhibit initiation or functionally associate with the PICs. Gdown1 does associate with pol II during the early stage of transcript elongation but this association is competitive with TFIIF. By phosphorylating TFIIF, PICs can be assembled that do not retain TFIIF. Gdown1 also fails to functionally associate with these TFIIF-less PICs, but once polymerase enters transcript elongation, complexes lacking TFIIF quantitatively bind Gdown1. Our results provide a partial resolution of the paradox of the competition between Gdown1 and TFIIF for association with pol II. Although Gdown1 completely displaces TFIIF from free pol II and elongation complexes, Gdown1 does not functionally associate with the PIC. Gdown1 can enter the transcription complex immediately after initiation. Modification of TFIIF provides one pathway through which efficient Gdown1 loading can occur early in elongation, allowing downstream pausing to be regulated.
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