ArticleMolecular and cellular biology1992
Stability of Drosophila RNA polymerase II elongation complexes in vitro.
Article in Molecular and cellular biology, 1992. 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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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
35 citing papers in PubMed, 62 citations in OpenAlex.
- The Promoter-Proximal Pause: A Decision Point Governing RNA Polymerase II Fate.Annual review of biochemistry · 2026Review
- CDK9: A Comprehensive Review of Its Biology, and Its Role as a Potential Target for Anti-Cancer Agents.Frontiers in oncology · 2021Review
- RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.Chemical reviews · 2013Review
- Review
- Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans.Nature reviews. Genetics · 2012Review
- Estrogen receptor-α recruits P-TEFb to overcome transcriptional pausing in intron 1 of the MYB gene.Nucleic acids research · 2012Article
- Identification and validation of protein targets of bioactive small molecules.Bioorganic & medicinal chemistry · 2012Review
- Pol II waiting in the starting gates: Regulating the transition from transcription initiation into productive elongation.Biochimica et biophysica acta · 2011Review
- Global analysis of short RNAs reveals widespread promoter-proximal stalling and arrest of Pol II in Drosophila.Science (New York, N.Y.) · 2010Article
- Isolation and functional analysis of RNA polymerase II elongation complexes.Methods (San Diego, Calif.) · 2009Article
- NELF and DSIF cause promoter proximal pausing on the hsp70 promoter in Drosophila.Genes & development · 2003Article
- Cotranscriptional processing of Drosophila histone mRNAs.Molecular and cellular biology · 2003Article
- Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription.Nucleic acids research · 2001Article
- Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster.Genes & development · 2000Article
- Discrete promoter elements affect specific properties of RNA polymerase II transcription complexes.Nucleic acids research · 2000Article
- P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II.Molecular and cellular biology · 2000Review
- Tat activates human immunodeficiency virus type 1 transcriptional elongation independent of TFIIH kinase.Molecular and cellular biology · 1999Article
- The binding of the alpha subunit of protein kinase CK2 and RAP74 subunit of TFIIF to protein-coding genes in living cells is DRB sensitive.Molecular and cellular biochemistry · 1999Article
- Nucleosomes are not necessary for promoter-proximal pausing in vitro on the Drosophila hsp70 promoter.Nucleic acids research · 1998Article
- Mitotic repression of RNA polymerase II transcription is accompanied by release of transcription elongation complexes.Molecular and cellular biology · 1997Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We show that nuclear extract from Drosophila Kc cells supports efficient elongation by RNA polymerase II initiated from the actin 5C promoter. The addition of 0.3% Sarkosyl, 1 mg of heparin per ml, or 250 mM KCl immediately after initiation has two effects. First, the elongation rate is reduced 80 to 90% as a result of the inhibition of elongation factors. Second, there is an increase in the amount of long runoff RNA, suggesting that there is an early block to elongation that is relieved by the disruptive reagents. Consistent with the first effect, we find that the ability of factor 5 (TFIIF) to stimulate the elongation rate is inhibited by the disruptive agents when assayed in a defined system containing pure RNA polymerase II and a dC-tailed template. The disruptive agents also inhibit the ability of DmS-II to suppress transcriptional pausing but only slightly reduce the ability of DmS-II to increase the elongation rate twofold. The pause sites encountered by RNA polymerase II after initiation at a promoter and subsequent treatment with the disruptive reagents are also recognized by pure polymerase transcribing a dC-tailed template. It has been suggested that 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits RNA polymerase II during elongation, but we find that the purine nucleoside analog has no effect on elongation complexes containing RNA over 500 nucleotides in length or on the action of factor 5 or DmS-II in the defined system.
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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.